美国博纯技术手册(2014版)
microflexOperatorManual_Chinese
Nafion-美国博纯
Nafion®是聚四氟乙烯（Teflon®）和全氟-3，6-二环氧-4-甲基-7-癸烯-硫酸的共聚物。
简单说,是Teflon结构伴有另一氟碳临时侧链。
侧链的终点是一个磺酸基（- SO3H）。
如同大部分的含氟聚合物一样，Nafion具有极强的抗化学侵蚀性（抗腐蚀）。
磺酸基（- SO3H）固定在氟碳基上，不会被移除。
Nafion重要特性如下：耐腐蚀Nafion®是聚四氟乙烯[Teflon®]和全氟-3，6-二环氧-4-甲基-7-癸烯-硫酸的共聚物，象Teflon一样，Nafion®具有极强的抗化学侵蚀特性，所以它能被用于强酸性气体的场合。
快速因为含有磺酸基团，Nafion®具有极强的渗水性。
在此化学结构中，磺酸基最多可以接受13个水份子。
通过磺酸基团，在Nafion®管壁上形成了一个交联的离子通道，水在管壁表面经过磺酸基吸收后，通过离子通道迅速地转移至管壁的另一面，然后蒸发。
选择性与微孔渗透膜是一种相对较慢的扩散过程不同，Nafion®对水份的吸收和转移是非常迅速的水合过程。
这是一个只和水发生的特殊化学反应，其他物质通常不会受到影响。
过程简单—当水份在气相的状态下由管内转移到管外，没有自由能的变化，所以不需要额外的能量来驱动该反应。
反应的驱动力来源于管内和管外的水份浓度差（湿度差）。
过程简单当水份在气相的状态下由管内转移到管外，没有自由能的变化，所以不需要额外的能量来驱动该反应。
反应的驱动力来源于管内和管外的水份浓度差（湿度差）。
美国博纯公司是经杜邦独家授权唯一的Nafion管材制造商。
博纯从杜邦公司购买Nafion树脂技术，制造管材，并通过复杂的化学处理来激活它。
博纯利用Nafion对水的传输性质生产了不同类型的干燥器和加湿器，从研究模块到干燥系统。
博纯也为干燥应用以外的其他应用提供Nafion管材。
promega 组织和毛发提取试剂盒（与DNA IQ TM 系统结合使用）说明书
组织和毛发提取试剂盒（与DNA IQ TM系统结合使用）操作手册本说明书用于产品DC6740所有的技术文献均可从公司网站得到请访问公司网站以证实您所使用的技术手册为最新版本I．介绍 (1)III. 产品组分 (2)III．组织和毛发提取试剂盒与 DNA IQ TM系统结合使用的操作步骤 (2)A．试剂的准备 (2)B．从发囊及发根中纯化DNA (5)C．从新鲜组织、冰冻组织、甲醛固定组织及石蜡包埋组织中纯化DNA (6)IV．疑难解答 (7)V．参考文献 (7)VI．相关产品 (8)I.介绍Promega的 DNA IQ TM系统使用一种新的顺磁性树脂来纯化DNA, 该试剂盒中包含有DNA纯化所需的可用于多种形式样品的高效裂解液。
然而，DNA IQ TM 系统中的裂解液对一些如组织和毛发的样品不能有效地裂解，这些样品需要蛋白酶K的预处理以协助样品的裂解。
组织和毛发提取试剂盒（与DNA IQ TM系统结合使用）中提供的试剂和操作手册可用于大部分组织和毛发的有效裂解，除去样品中的蛋白和其它成分，随后用DNA IQ TM系统对样品中的DNA进行纯化。
基因组和线粒体DNA结合使用组织和毛发提取试剂盒（与DNA IQ TM系统结合使用）及DNA IQ TM系统，可高效地从样品中提取纯化双链或单链基因组DNA及线粒体DNA。
如果待提取的样品被微生物污染，则微生物DNA被一起分离。
可抑制PCR扩增的小于 80bp的 DNA可被选择性地去除，从而使纯化的 DNA更有效地用于 PCR扩增。
组织和毛发提取试剂盒（与DNA IQ TM系统结合使用）可提高 DNA纯化的产量当用DNA IQ TM系统—数据库操作手册（TB297）中涉及的样品进行 DNA纯化时，DNA IQ TM系统所提取的 DNA的量是固定的，约 100ng。
对于不同检材中DNA的定量提取依赖于样品中超量的DNA饱和DNA IQ TM 树脂。
在结合使用组织和毛发提取试剂盒（与DNA IQ TM系统结合使用）及 DNA IQ TM系统时，若用蛋白酶K消化去除竞争结合DNA IQ TM 树脂的物质，则树脂从蛋白酶K处理过的注意：本中文操作手册仅供实验参考，在实际使用中请详细对照原英文技术手册TB307。
Cascada RO中文手册.
Cascada™实验室用水纯化系统RO-water型号本手册为如下型号的Cascada TM实验水系统模型的安装、操作和维护指南：Cascada™ RO-Water纯化装置可提供实验室、医药业和工业应用的基准级纯水安装、操作和维护上述系统之前，请阅读本手册。
如不遵守本手册中的说明，则产品性能和/或用户安全可能无法达到预期水平。
小心拆下包装，仔细检查所有系统部件，以确保这些部件在运输过程没有发生损坏。
用户可从当地颇尔办事处或经销商获取售后服务支持或购买消耗性部件。
关于客户服务联系方式的详细信息，请参阅本书结尾部分。
安全说明 4 用户责任 4 电气性能 4 压力 5 消毒药品 5 控制危害健康的物质 5简介产品说明 6 水纯化系统流程 6技术规格8控制10安装说明11 拆开包装11 定位11 连接13 控制参数的初次设定15 显示及更换计时设定17 初次运行18 操作19 报警情况19 维护20 更换预处理过滤胶囊（部件编号：PAL-LC140）21 清洗入水口粗滤器22 更换逆渗透过滤胶囊（部件编号：PAL-LC143）22消毒程序23 消毒23 消毒药片（部件编号：PAL-CT1）-安全性相关资讯24疑难解答25耗材和附件26控制面板的要点27 图标27 报警情况27 更换计时28 水质报警待机28担保/销售条款：29联络信息30用户责任请事先通读本操作手册，再着手进行系统的运行或维护。
本操作手册中陈述的安全性基本准则，旨在作为颇尔公司出品装置的安全操作指南。
通用安全信息，连同针对特定机器而明确规定的保养、维护、操作材料，共同构成本操作手册的完整性，二者缺一不可。
任何操作人员、维修人员，或以任何方式涉及此装置的人员，在开始工作前，必须完全熟悉这些信息。
用户有责任确保本操作手册中阐述的规程得到很好的遵循。
从设计角度而言，Cascada™实验室用水纯化系统具备相当的安全性；然而，这些装置的作业人员也应当了解一切可能存在的安全性隐患，这一点至关重要。
2009版《AATCC技术手册》发布
2009版《AATCC技术手册》发布
佚名
【期刊名称】《印染》
【年(卷),期】2009(35)11
【摘要】日前，美国AATCC（美国染色与化学家协会）正式发布了2009版的《AATCC技术手册》。
该手册包括112个现行有效的测试方法标准、11个评价程序及专论，与2008版相比，新版手册减少了4个标准。
【总页数】2页(P53-54)
【关键词】AATCC;技术手册;测试方法标准;评价程序;化学家;美国;染色
【正文语种】中文
【中图分类】TS197;TP391
【相关文献】
1.2008版〈AATCC技术手册〉中文版面市 [J],
2.2009版《AATCC技术手册》五大变化 [J], 傅科杰
3.AATCC技术手册更新 [J],
4.2008版AATCC技术手册发布 [J],
因版权原因，仅展示原文概要，查看原文内容请购买。
Clarus 500 MS manual
C l a r u s500M a s sG C M a s s S p e c t r o m e t e rPerkin Elmer气相层析质谱仪Clarus 500 MS中文操作手册Perkin Elmer 气相层析质谱仪Clarus 500 Mass开机步骤1. 确定所有的接线都正确1.检视所有的电线接头及气体管路都已正确连结2.确定GC 的载流气体已开，且压力正常3.确定GC 注射口之垫片完整2. 激活Clarus 500 MS 软件1.重复按下Clarus 500 MS 之Icon ，会出现Clarus 500 Mass Login 屏幕The Clarus 500 Mass Login screen appears:2.输入密码及键入OK3.出现Clarus 500 Mass 初始之Sample List 屏幕Turbomass 軟體The initial Clarus 500 Mass screen of the Sample List appears:3. 按将Tune Page打开The default Tune page appears:4. 如果仪器尚未抽真空，按下Other选项中之Pump激活Pump这个动作将会激活forepump及High vacuum pump，如果您的Clarus 500 Mass装观看Pirani及Penning gauge之读值，将载流气体有真空压力计，可按下He流速设定1 ml/min，配备为Turbomolecular pump时需等待5分钟，若为Diffusion pump系统则需等待20分钟，真空度才能达到3.0 ╳ 10-5 Torr 。
5. 当注射口为CAP或PSS时，将GC split flow设为50 ml/min 如果使用Clarus 500 Mass 控制GC，则以下列步骤设定1.按下则出现Acquisition Control Panel屏幕2.选择GC选项中的Release Control3.重复按GC 仪器键盘上的[Inject Prog]键，直到流速显示页出现。
韩国TCK公司技术手册 0前言
前言韩国TCK公司是当今世界上少有的几个能大规模生产卷式反渗透复合膜元件的膜制造商之一；韩国TCK公司生产的CSM系列反渗透分离膜以其卓越的性能而驰名国内外，并在国内外水处理行业中被广泛使用，本资料就是为向广大用户介绍CSM反渗透膜元件而专门编写的。
反渗透膜系统作为一个典型的膜分离操作单元，已被广泛应用于生活饮用水净化、电子行业超纯水生产、化工、电力、纺织、冶金等行业工艺用水的生产过程中，在水处理领域占有十分重要的地位。
因此，为使中国的反渗透水处理工程公司和用户能对CSM反渗透膜技术及应用技术有着更深刻的了解，特地用中文编辑并出版该资料，以供广大水处理工程公司、设计单位和反渗透膜用户在设计及使用时参考。
本刊在此主要编辑了CSM反渗透膜产品性能介绍、反渗透预处理工艺、膜系统设计导则、CSM反渗透膜与其他公司同类产品性能对比等有关内容。
随着CSM反渗透膜在国内各行业应用的不断深入，我们也将不断地完善本刊，补充更新、更多的内容，希望本刊能成为您在反渗透系统设计及应用工作中的助手。
尽管我们所编辑的资料在很多方面存在不足。
但我们真诚地希望它能对从事水处理行业的各位同仁了解反渗透水处理技术有所裨益。
为此，我们真诚地希望参考本资料和使用反渗透膜产品的诸位提出宝贵的建议。
韩国TCK公司CSM膜事业部目录1.韩国TCK公司介绍1-1.总部和工厂地址 (1)1-2.韩国TCK公司的历史 (2)1-3.反渗透膜业务历史 (4)2.反渗透介绍2-1.反渗透技术应用概述 (5)2-2.反渗透的原理 (6)2-3.反渗透的类型 (7)2-4.CSM反渗透膜特点 (9)2-5.CSM反渗透膜脱盐率特点 (11)3.CSM膜技术详述3-1.CSM膜元件命名法 (13)3-2.CSM膜全球部分业绩 (14)3-3.苦咸水膜元件 (17)3-4.抗污染膜元件 (20)3-5.超低压节能膜元件 (23)3-6.海水淡化膜元件 (26)3-7.纳滤膜元件 (29)3-8.自来水膜元件 (31)3-9.超纯水膜元件 (33)3-10.家用膜元件 (34)4.水化学和系统预处理4-1.介绍 (35)4-2.进水水质分析 (36)4-3.防止结垢形成 (44)4-4.防止硅垢 (51)4-5.胶体污染的控制 (54)4-6.生物污染的防范 (58)4-7.有机物污染的防治 (61)5.系统设计5-1.介绍 (62)5-2.系统设计指南 (63)5-3.间歇式和连续式工艺 (65)5-4.单支压力容器系统 (67)5-5.单段系统 (68)5-6.多段系统 (69)5-7.双级反渗透系统 (70)5-8.系统的膜元件数量和压力容器数量的设计 (71)5-9.特殊应用系统的测试 (74)6.系统运行6-1.介绍 (75)6-2.试运行 (76)6-3.运行管理记录 (79)6-4.数据标准化 (82)6-5.控制反渗透系统的微生物生长 (87)7.化学清洗和杀菌7-1.介绍 (88)7-2.定时的化学清洗 (89)7-3.清洗装置 (90)7-4.清洗程序 (91)7-5.清洗的化学药品 (93)7-6.杀菌 (97)8.故障诊断和排除8-1.介绍 (99)8-2.仪表的校正 (100)8-3.确定系统脱盐率低的原因 (102)8-4.膜元件分析 (103)8-5.重度污染膜元件的清洗检测 (104)8-6.重度污染的膜元件的分析方法 (105)8-7.问题原因和纠正方法 (107)9.附录9-1.品质保证条件 (116)9-2.反渗透系统运行前的检查程序 (122)9-3.反渗透的运行记录 (124)9-4.各种离子化学单位之间的转换 (125)9-5.标准海水成份 (126)9-6.难溶盐溶度积 (127)9-7.各种酸溶液电导 (128)9-8.各种碱溶液的电导 (128)9-9.盐溶液的电导 (129)9-10.各种离子的电导 (130)9-11.各种浓度的氯化钠溶液的电导 (131)9-12.25℃时碳酸氢根和二氧化碳的转化曲线 (131)9-13.各种浓度的氯化纳溶液的渗透压 (132)9-14.各种盐溶液的渗透压 (132)9-15.CSM膜的性能曲线 (133)9-16.温度校正系数(TCF) (138)9-17.CSM抗污染膜 (141)9-18.抗污染膜的性能参数 (147)10.认证书。
蛋白质纯化手册【ProteinPurificationHandbook】
Protein PurificationHandbook18-1132-29Edition ABHiTrap, Sepharose, STREAMLINE, Sephadex, MonoBeads, Mono Q,Mono S, MiniBeads, RESOURCE, SOURCE, Superdex, Superose, HisTrap, HiLoad, HiPrep, INdEX, BPG, BioProcess, FineLINE, MabTrap, MAbAssistant, Multiphor, FPLC, PhastSystem and ÄKTA are trademarks of Amersham Pharmacia Biotech Limitedor its subsidiaries.Amersham is a trademark of Nycomed Amersham plcPharmacia and Drop Design are trademarks of Pharmacia & Upjohn Inc Coomassie is a trademark of ICI plcAll goods and services are sold subject to the terms and conditions of sale of the company within the Amersham Pharmacia Biotech group which supplies them. A copy of these terms and conditions of sale is available on request.© Amersham Pharmacia Biotech AB 1999-All rights reserved.Amersham Pharmacia Biotech ABSE-751 84 Uppsala SwedenAmersham Pharmacia Biotech UK Limited Amersham Place Little Chalfont Buckinghamshire England HP7 9NA Amersham Pharmacia Biotech Inc800 Centennial Avenue PO Box 1327 Piscataway NJ 08855 USAProtein Purification HandbookContents Introduction (7)Chapter 1Purification Strategies - A Simple Approach (9)Preparation (10)Three Phase Purification Strategy (10)General Guidelines for Protein Purification (12)Chapter 2 Preparation (13)Before You Start (13)Sample Extraction and Clarification (16)Chapter 3Three Phase Purification Strategy (19)Principles (19)Selection and Combination of Purification Techniques (20)Sample Conditioning (26)Chapter 4Capture (29)Chapter 5Intermediate Purification (37)Chapter 6Polishing (40)Chapter 7Examples of Protein Purification Strategies (45)Three step purification of a recombinant enzyme (45)Three step purification of a recombinant antigen binding fragment (49)Two step purification of a monoclonal antibody (54)One step purification of an integral membrane protein (57)Chapter 8Storage Conditions (61)Extraction and Clarification Procedures (62)Chapter 9Principles and Standard Conditions for Purification Techniques (73)Ion exchange (IEX) (73)Hydrophobic interaction (HIC) (79)Affinity (AC) (85)Gel filtration (GF) (88)Reversed phase (RPC) (92)Expanded bed adsorption (EBA) (95)IntroductionThe development of techniques and methods for protein purification has been an essential pre-requisite for many of the advancements made in biotechnology. This booklet provides advice and examples for a smooth path to protein purification. Protein purification varies from simple one-step precipitation procedures to large scale validated production processes. Often more than one purification step is necessary to reach the desired purity. The key to successful and efficient protein purification is to select the most appropriate techniques, optimise their performance to suit the requirements and combine them in a logical way to maximise yield and minimise the number of steps required.Most purification schemes involve some form of chromatography. As a result chromatography has become an essential tool in every laboratory where protein purification is needed. The availability of different chromatography techniques with different selectivities provides a powerful combination for the purification of any biomolecule.Recombinant DNA developments over the past decade have revolutionised the production of proteins in large quantities. Proteins can even be produced in forms which facilitate their subsequent chromatographic purification. However, this has not removed all challenges. Host contaminants are still present and problems related to solubility, structural integrity and biological activity can still exist. Although there may appear to be a great number of parameters to consider, with a few simple guidelines and application of the Three Phase Purification Strategy the process can be planned and performed simply and easily, with only a basic knowledge of the details of chromatography techniques.78Chapter 1Purification Strategies- a simple approachApply a systematic approach to development of a purification strategy. The first step is to describe the basic scenario for the purification. General considerations answer questions such as: What is the intended use of the product? What kind of starting material is available and how should it be handled? What are the purity issues in relation to the source material and intended use of the final product? What has to be removed? What must be removed completely? What will be the final scale of purification? If there is a need for scale-up, what consequences will this have on the chosen purification techniques? What are the economical constraints and what resources and equipment are available?Most purification protocols require more than one step to achieve the desired level of product purity. This includes any conditioning steps necessary to transfer the product from one technique into conditions suitable to perform the next technique. Each step in the process will cause some loss of product. For example, if a yield of 80% in each step is assumed, this will be reduced to only 20% overall yield after 8 processing steps as shown in Figure 1. Consequently, to reach the targets for yield and purity with the minimum number of steps and the simplest possible design, it is not efficient to add one step to another until purity requirements have been fulfilled. Occasionally when a sample is readily available purity can be achieved by simply adding or repeating steps. However, experience shows that, even for the most challenging applications, high purity and yield can be achieved efficiently in fewer than four well-chosen and optimised purification steps. Techniques should be organised in a logical sequence to avoid the need for conditioning steps and the chromatographic techniques selected appropriately to use as few purification steps as possible.Limit the number of steps in a purification procedure910Fig.1.Yields from multi-step purifications.PreparationThe need to obtain a protein, efficiently, economically and in sufficient purity and quantity, applies to every purification. It is important to set objectives for purity,quantity and maintenance of biological activity and to define the economical and time framework for the work. All information concerning properties of the target protein and contaminants will help during purification development. Some simple experiments to characterise the sample and target molecule are an excellent investment. Development of fast and reliable analytical assays is essential to follow the progress of the purification and assess its effectiveness. Sample preparation and extraction procedures should be developed prior to the first chromatographic purification step.With background information, assays and sample preparation procedures in place the Three Phase Purification Strategy can be considered.Three Phase Purification Strategy Imagine the purification has three phases Capture, IntermediatePurification and Polishing.In the Three Phase Strategy specific objectives are assigned to each step within the process:In the capture phase the objectives are to isolate, concentrate and stabilise the target product.During the intermediate purification phase the objective is to remove most of the bulk impurities such as other proteins and nucleic acids, endotoxins and viruses.In the polishing phase the objective is to achieve high purity by removing any remaining trace impurities or closely related substances.The selection and optimum combination of purification techniques for Capture,Intermediate Purification and Polishing is crucial to ensure fast method development, a shorter time to pure product and good economy.108060402012345678Number of steps 95% / step90% / step 85% / step 80% / step 75% / stepYield (%)The final purification process should ideally consist of sample preparation, including extraction and clarification when required, followed by three major purification steps, as shown in Figure 2. The number of steps used will always depend upon the purity requirements and intended use for the protein.Fig. 2.Preparation and the Three Phase Purification Strategy11Guidelines for Protein PurificationThe guidelines for protein purification shown here can be applied to any purification process and are a suggestion as to how a systematic approach can be applied to the development of an effective purification strategy. As a reminder these guidelines will be highlighted where appropriate throughout the following chapters.Define objectivesfor purity, activity and quantity required of final product to avoid over or under developing a methodDefine properties of target protein and critical impuritiesto simplify technique selection and optimisationDevelop analytical assaysfor fast detection of protein activity/recovery and to work efficientlyMinimise sample handling at every stageto avoid lengthy procedures which risk losing activity/reducing recovery Minimise use of additivesadditives may need to be removed in an extra purification step or may interfere with activity assaysRemove damaging contaminants earlyfor example, proteasesUse a different technique at each stepto take advantage of sample characteristics which can be used for separation (size, charge, hydrophobicity, ligand specificity)Minimise number of stepsextra steps reduce yield and increase time, combine steps logicallyKEEP IT SIMPLE!12Chapter 2PreparationBefore You StartThe need to obtain a protein, efficiently, economically and in sufficient purity and quantity, applies to any purification, from preparation of an enriched protein extract for biochemical characterisation to large scale production of a therapeutic recombinant protein. It is important to set objectives for purity and quantity, maintenance of biological activity and economy in terms of money and time. Purity requirements must take into consideration the nature of the source material, the intended use of the final product and any special safety issues. For example, it is important to differentiate between contaminants which must be removed and those which can be tolerated. Other factors can also influence the prioritisation of objectives. High yields are usually a key objective, but may be less crucial in cases where a sample is readily available or product is required only in small quantities. Extensive method development may be impossible without resources such as an ÄKTA™design chromatography system. Similarly, time pressure combined with a slow assay turnaround will steer towards less extensive scouting and optimisation. All information concerning properties of the target protein and contaminants will help during purification development, allowing faster and easier technique selection and optimisation, and avoiding conditions which may inactivate the target protein.Development of fast and reliable analytical assays is essential to follow the progress of the purification and assess effectiveness (yield, biological activity, recovery).Define objectivesGoal:To set minimum objectives for purity and quantity, maintenance of biological activity and economy in terms of money and time.Define purity requirements according to the final use of the product. Purity requirement examples are shown below.Extremely high > 99%Therapeutic use, in vivo studiesHigh 95- 99 %X-ray crystallography and most physico-chemicalcharacterisation methodsModerate < 95 %Antigen for antibody productionN-terminal sequencing13Identify 'key' contaminantsIdentify the nature of possible remaining contaminants as soon aspossible.The statement that a protein is >95% pure (i.e. target protein constitutes 95% of total protein) is far from a guarantee that the purity is sufficient for an intended application. The same is true for the common statement "the protein was homogenous by Coomassie™ stained SDS-PAGE". Purity of 95% may be acceptable if the remaining 5% consists of harmless impurities. However, even minor impurities which may be biologically active could cause significant problems in both research and therapeutic applications. It is therefore important to differentiate between contaminants which must be removed completely and those which can be reduced to acceptable levels. Since different types of starting material will contain different contaminant profiles they will present different contamination problems.It is better to over-purify than to under-purify.Although the number of purification steps should be minimised, thequality of the end product should not be compromised. Subsequent results might be questioned if sample purity is low and contaminants are unknown.Contaminants which degrade or inactivate the protein or interfere withanalyses should be removed as early as possible.The need to maintain biological activity must be considered at every stage during purification development. It is especially beneficial if proteases are removed and target protein transferred into a friendly environment during the first step.Economy is a very complex issue. In commercial production the time to market can override issues such as optimisation for recovery, capacity or speed. Robustness and reliability are also of great concern since a batch failure can have major consequences.It may be necessary to use analytical techniques targetted towards specific conta-minants in order to demonstrate that they have been removed to acceptable levels. 14Define properties of target protein and critical impurities Goal:To determine a 'stability window' for the target protein for easier selection and optimisation of techniques and to avoid protein inactivation during purification.Check target protein stability window for at least pH and ionic strength. All information concerning the target protein and contaminant properties will help to guide the choice of separation techniques and experimental conditions for purification. Database information for the target, or related proteins, may give size, isoelectric point (pI) and hydrophobicity or solubility data. Native one and two dimensional PAGE can indicate sample complexity and the properties of the target protein and major contaminants. Particularly important is a knowledge of the stability window of the protein so that irreversible inactivation is avoided. Itis advisable to check the target protein stability window for at least pH and ionic strength. Table 1 shows how different target protein properties can affect a purification strategy.Table 1.Protein properties and their effect on development of purification strategies. Sample and target protein properties Influence on purification strategyTemperature stability Need to work rapidly at lowered temperaturepH stability Selection of buffers for extraction and purificationSelection of conditions for ion exchange, affinity orreversed phase chromatographyOrganic solvents stability Selection of conditions for reversed phasechromatographyDetergent requirement Consider effects on chromatographic steps and the needfor detergent removal. Consider choice of detergent.Salt (ionic strength)Selection of conditions for precipitation techniques andhydrophobic interaction chromatographyCo-factors for stability or activity Selection of additives, pH, salts, buffersProtease sensitivity Need for fast removal of proteases or addition ofinhibitorsSensitivity to metal ions Need to add EDTA or EGTA in buffersRedox sensitivity Need to add reducing agentsMolecular weight Selection of gel filtration mediaCharge properties Selection of ion exchange conditionsBiospecific affinity Selection of ligand for affinity mediumPost translational modifications Selection of group specific affinity medium Hydrophobicity Selection of medium for hydrophobic interactionchromatography15Develop analytical assaysGoal:To follow the progress of a purification, to assess effectiveness (yield, biological activity, recovery) and to help during optimisation.Select assays which are fast and reliable.To progress efficiently during method development the effectiveness of each step should be assessed. The laboratory should have access to the following assays:• A rapid, reliable assay for the target protein• Purity determination• Total protein determination• Assays for impurities which must be removedThe importance of a reliable assay for the target protein cannot be over- emphasised. When testing chromatographic fractions ensure that the buffers used for separation do not interfere with the assay. Purity of the target protein is most often estimated by SDS-PAGE, capillary electrophoresis, reversed phase chromatography or mass spectrometry. Lowry or Bradford assays are used most frequently to determine the total protein.The Bradford assay is particularly suited to samples where there is a high lipid content which may interfere with the Lowry assay.For large scale protein purification the need to assay for target proteins and critical impurities is often essential. In practice, when a protein is purified for research purposes, it is too time consuming to identify and set up specific assays for harmful contaminants. A practical approach is to purify the protein to a certain level, and then perform SDS-PAGE after a storage period to check for protease cleavage. Suitable control experiments, included within assays forbio-activity, will help to indicate if impurities are interfering with results.Sample Extraction and Clarification Minimise sample handlingMinimise use of additivesRemove damaging contaminants earlyDefinition:Primary isolation of target protein from source material.Goal:Preparation of a clarified sample for further purification. Removal of particulate matter or other contaminants which are not compatible with chromatography.16The need for sample preparation prior to the first chromatographic step is dependent upon sample type. In some situations samples may be taken directly to the first capture step. For example cell culture supernatant can be applied directly to a suitable chromatographic matrix such as Sepharose™ Fast Flow and may require only a minor adjustment of the pH or ionic strength. However, it is most often essential to perform some form of sample extraction and clarification procedure.If sample extraction is required the chosen technique must be robust and suitable for all scales of purification likely to be used. It should be noted that a technique such as ammonium sulphate precipitation, commonly used in small scale, may be unsuitable for very large scale preparation. Choice of buffers and additives must be carefully considered if a purification is to be scaled up. In these cases inexpensive buffers, such as acetate or citrate, are preferable to the more complex compositions used in the laboratory. It should also be noted that dialysis and other common methods used for adjustment of sample conditions are unsuitable for very large or very small samples.For repeated purification, use an extraction and clarification techniquethat is robust and able to handle sample variability. This ensures areproducible product for the next purification step despite variability instarting material.Use additives only if essential for stabilisation of product or improvedextraction. Select those which are easily removed. Additives may need tobe removed in an extra purification step.Use pre-packed columns of Sephadex™ G-25 gel filtration media, forrapid sample clean-up at laboratory scale, as shown in Table 2.Table 2.Pre-packed columns for sample clean-up.Pre-packed column Sample volume Sample volume Code No.loading per run recovery per runHiPrep™Desalting 26/10 2.5 -15 ml7.5 - 20 ml17-5087-01HiTrap Desalting0.25 - 1.5 ml 1.0 - 2.0 ml17-1408-01Fast Desalting PC 3.2/100.05 - 0.2 ml0.2 - 0.3 ml17-0774-01PD-10 Desalting 1.5 - 2.5 ml 2.5 - 3.5 ml17-0851-01 Sephadex G-25 gel filtration media are used at laboratory and production scale for sample preparation and clarification of proteins >5000. Sample volumes of up to 30%, or in some cases, 40% of the total column volume are loaded. In a single step, the sample is desalted, exchanged into a new buffer, and low molecular weight materials are removed. The high volume capacity, relative insensitivity to sample concentration, and speed of this step enable very large sample volumes to be processed rapidly and efficiently. Using a high sample volume load results in a separation with minimal sample dilution (approximately 1:1.4). Chapter 8 contains further details on sample storage, extraction and clarification procedures.17Sephadex G-25 is also used for sample conditioning i.e. rapid adjustment of pH, buffer exchange and desalting between purification steps.Sephadex G-25 gel filtrationFor fast group separations between high and low molecular weight substances Typical flow velocity 60 cm/h (Sephadex G-25 SuperFine, Sephadex G-25 Fine), 150 cm/h (Sephadex G-25 Medium).If large sample volumes will be handled or the method scaled-up in the future, consider using STREAMLINE™ expanded bed adsorption. This technique is particularly suited for large scale recombinant protein and monoclonal antibody purification. The crude sample containing particles can be applied to the expanded bed without filtration or centrifugation. STREAMLINE adsorbents are specially designed for use in STREAMLINE columns. Together they enable the high flow rates needed for high productivity in industrial applications of fluidised beds. The technique requires no sample clean up and so combines sample preparation and capture in a single step. Crude sample is applied to an expanded bed STREAMLINE media. Target proteins are captured whilst cell debris, cells, particulate matter, whole cells, and contaminants pass through. Flow is reversed and the target proteins are desorbed in the elution buffer.STREAMLINE (IEX, AC, HIC)For sample clean-up and capture direct from crude sample.STREAMLINE adsorbents are designed to handle feed directly from both fermentation homogenate and crude feedstock from cell culture/fermentation at flow velocities of 200 - 500 cm/h, according to type and application.Particle size: 200 µmNote:cm/h: flow velocity (linear flow rate) = volumetric flow rate/cross sectional area of column.18Chapter 3Three Phase Purification StrategyPrinciplesWith background information, assays, and sample preparation and extraction procedures in place the Three Phase Purification Strategy can be applied (Figure 3). This strategy is used as an aid to the development of purification processes for therapeutic proteins in the pharmaceutical industry and is equally efficient as an aid when developing purification schemes in the research laboratory.Fig. 3.Preparation and the Three Phase Purification Strategy.Assign a specific objective to each step within the purification process.In the Three Phase Strategy a specific objective is assigned to each step. The purification problem associated with a particular step will depend greatly upon the properties of the starting material. Thus, the objective of a purification step will vary according to its position in the process i.e. at the beginning for isolation of product from crude sample, in the middle for further purification of partially purified sample, or at the end for final clean up of an almost pure product.The Three Phase Strategy ensures faster method development, a shorter time to pure product and good economy.In the capture phase the objectives are to isolate, concentrate and stabilise the target product. The product should be concentrated and transferred to an environment which will conserve potency/activity. At best, significant removal of other critical contaminants can also be achieved.19During the intermediate purification phase the objectives are to remove most of the bulk impurities,such as other proteins and nucleic acids, endotoxins and viruses.In the polishing phase most impurities have already been removed except for trace amounts or closely related substances. The objective is to achieve final purity.It should be noted that this Three Phase Strategy does not mean that all strategies must have three purification steps. For example, capture and intermediate purification may be achievable in a single step, as may intermediate purification and polishing. Similarly, purity demands may be so low that a rapid capture step is sufficient to achieve the desired result, or the purity of the starting material may be so high that only a polishing step is needed. For purification of therapeutic proteins a fourth or fifth purification step may be required to fulfil the highest purity and safety demands.The optimum selection and combination of purification techniques for Capture, Intermediate Purification and Polishing is crucial for an efficient purification process.Selection and Combination ofPurification TechniquesMinimise sample handlingMinimise number of stepsUse different techniques at each stepGoal:Fastest route to a product of required purity.For any chromatographic separation each different technique will offer different performance with respect to recovery, resolution, speed and capacity. A technique can be optimised to focus on one of these parameters, for example resolution, or to achieve the best balance between two parameters, such as speed and capacity.A separation optimised for one of these parameters will produce results quite different in appearance from those produced using the same technique, but focussed on an alternative parameter. See, for example, the results shown on page 49 where ion exchange is used for a capture and for a polishing step.20Select a technique to meet the objectives for the purification step. Capacity,in the simple model shown, refers to the amount of target protein loaded during purification. In some cases the amount of sample which can be loaded may be limited by volume (as in gel filtration) or by large amounts of contaminants rather than the amount of the target protein.Speed is of the highest importance at the beginning of a purification where contaminants such as proteases must be removed as quickly as possible. Recovery becomes increasingly important as the purification proceeds because of the increased value of the purified product. Recovery is influenced by destructive processes in the sample and unfavourable conditions on the column. Resolution is achieved by the selectivity of the technique and the efficiency of the chromatographic matrix to produce narrow peaks. In general, resolution is most difficult to achieve in the final stages of purification when impurities and target protein are likely to have very similar properties.Every technique offers a balance between resolution, speed, capacity and recovery and should be selected to meet the objectives for each purification step. In general, optimisation of any one of these four parameters can only be achieved at the expense of the others and a purification step will be a compromise. The importance of each parameter will vary depending on whether a purification step is used for capture, intermediate purification or polishing. This will steer the optimisation of the critical parameters, as well as the selection of the most suitable media for the step.Proteins are purified using chromatographic purification techniques which separate according to differences in specific properties, as shown in Table 3. Table 3.Protein properties used during purification.Protein property TechniqueCharge Ion exchange (IEX)Size Gel filtration (GF)Hydrophobicity Hydrophobic interaction (HIC),reversed phase (RPC)Biorecognition (ligand specificity)Affinity (AC)Charge, ligand specificity or hydrophobicity Expanded bed adsorption (EBA) follows theprinciples of AC, IEX or HIC21。
用户参考手册中文版
MilkoScan FT-120乳品分析仪用户参考手册Foss China Application Team2004年3月1 简介MilkoScan FT—120乳品分析仪是一台专门用于生产过程控制，成品控制以及按值论价的仪器。
本仪器在测量原乳和成品乳制品成分方面远远优于其它分析测定方法，在样品分析前，它只需对样品进行一次最小量的处理过程。
FT—120乳品分析仪包括两个主要部分：―测量部分―可完成全部操作控制的PC(个人计算机)测量部分和基本软件可以从福斯电子公司订购。
PC(个人计算机)可以在当地的市场上采购。
MilkoScan FT—120包括一个基本的配制，你可以根据需要增加软件和硬件模块，如果购买了MilkoScan Ft 120的基本模块，你可以通过添加模块来升级你的系统。
模块的总体图示见下：1.1有关这本手册这本Reference manual重点介绍技术资料及应用：－FTIR测量原理－定义产品程序－定标－统计术语及公式－应用指导－应用简报操作者手册同时和仪器一起提供，里面讲述了有关安装，维护和故障检查，化学试剂准备等。
备注：这本手册应用于MilkoScan FT 120，软件版本为1.4.0或更新版本，这版本基于Windows 98/NT设计，但是大多功能和用户界面与早期版本相同。
2设备工作原理2.1-2.3见操作手册第7章§2.4 FT－120乳品分析仪软件的许可证§2.4.1 软钥匙系统FT－120乳品分析仪软盘是以所有用户都可以得到完整程序的方式来设计的。
不想立即买的模块从程序中去除。
这可以通过一个由两个名叫“Site Code”和“site key”的新术语组成的软钥匙完成。
“Site Code”和“Site Key”都是由短的数字和字母组成，当第一次安装软盘时和用新的模块来升级FT－120乳品分析仪时，“Site Code”和“Site Key”必须在用户和福斯公司之间进行交换。
业界领先的燃料电池汽车动力系统采用博纯加湿器
由科 技 部 高 新 技 术 发展 及产 业 化 司 、 中国卫 星导航 系统专 项管理 办公 室 以及 上海 市科 学技术 委 员会 联 合 主办 的２ １ 上海 国际 智 能 交通 与 导 航产 ０ Ｏ 业 科技 发展论 坛９ １ 月 日在上 海会展 中心 拉开 帷幕 。 会 议现 场吸 引到 了政 府相 关机构 领导 、中外 顶级 演
透 到进 气 中进行 加湿 ，现在 全世 界只 有博纯 拥 有这种 专 利 技术 。由于 没有 活动 件 ，无需 能耗 ，也没 有元 器件 磨 损 、失效 和 泄露 的 问题 ，这 种 加湿 器可 以在 １ 级车 和３ 级 车 能够连 续运行 超过 １ ０ ４ 时 。 ０ ０＼ ０ 此外 ，博纯 加湿 器能承 受像 车辆 操作过 程 中遇到 的 振 动 ，如突然 启动 和刹 车 。这种 加湿器 即使 在温 度 变化
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讲 嘉 宾 和 上 百位 产 业 精 英 的 参 与 。论 坛 由 专 家演 讲 、互 动研讨 以及应 用展 览几部 分有机 组成 。智 能
交通与 卫星导 航作 为现代 高新技 术服务 产业 中 的重
宇 等 品牌 的行 业先 驱齐 集一堂 ，就 中国 实时交通 信息
业 界 领 先 的 燃 料 电池 汽 车 动 力 系 统 采 用 博 纯 加 湿器
近期 ，业 界领 先的某 燃料 电池汽 车动 力 系统公 司开 始采 用 美 国 博纯 （ ｅ ｍａ Ｐ ｒ ） 利 Ｆ Ｐ ｒ ｕｅ 专 Ｃ系 列 加 湿器 ， 用于 其燃料 电池 系统 中 。现 在 ，这批 燃料 电池 被安 装在
世 博 园专 用 的 燃料 电池 车 中 ，为 几 千 万 世博 园游 客 服
NASOPORE美国产品手册
NASOPORE美国产品手册NasoPore ?/OtoPore ?BioresorbableSolutionNasoPore ?/OtoPore ?Bioresorbable SolutionNasoPore ?Sinus (8/pkg)5400-010-0044cm Standard 5400-020-0044cm Firm5400-030-0044cm Extra Firm 5400-010-0088cm Standard 5400-020-0088cm Firm5400-030-0088cmExtra FirmOtoPore ?Ear Cylinder (8/pkg)5400-010-000Standard 5400-020-000FirmOtoPore ?Ear Square (8/pkg)5400-020-1004cm FirmIntended for the nasal and ear cavities as a temporary dressing.Stryker ?Neuro Spine ENT 4100East Milham Avenue Kalamazoo,MI 49001USA t:2693237700f:2693533026toll free:The information presented in this brochure is intendedto demonstrate the breadth of Stryker product offerings.Always refer to the package insert,product label and/or user instructions before using any Stryker product.Products may not be available in all markets.Productavailability is subject to the regulatory or medical practicesthat govern individual markets.Please contact your Stryker representative if you have questions about the availability of Stryker products in your area.Products referenced with TM designation are trademarks of Stryker.Products referenced with ?designation are registered trademarks of Stryker.Literature Number:9100-001-014Rev.B UnDe/P .S.Copyright ?2007Stryker Printed in USANasoPore ?/OtoPore ?Bioresorbable SolutionSinus Ear Cylinder Intended for the nasal and ear cavities as a temporarydressing.SinusThe most common procedures in which nasal dressing can be applied are:?EthmoidectomyMaxillary Antrostomy ?Sphenoidotomy ?Frontal Sinusotomy ?Septoplasty ?SMR FeaturesNo painful traumatic removalCan be easily cut and manipulated for surgeon’s useControlled compression of tissue ?Prevents adhesions/synechiae ?HemostaticRapid fragmentation to avoid risk of infection and TSS FragmentationNasoPore ?Sinus disappears completely within several days with predictable degradation.The biologically safe fragments are drained via the natural pathways.Outer/Middle EarThe most common procedures in which ear dressing can be applied are:?Tympanoplasty ?Myringoplasty ?Canalplasty Mastoid Surgery ?Stapes Surgery FeaturesCan be easily cut andmanipulated for surgeon’s useControlled compression of tissue and middle ear structures ?Prevents adhesions/synechiae FragmentationOtoPore ?Ear begins to dissolve within several days.Predictable degradationBreaks down into CO 2,H 2O,O 2,and polyamine (found in eukaryotic cells)Material Composition:NasoPore ?/OtoPore ?is entirely synthetic based ?Does not contain any organic components of unknown or processed materialEar Square上一页下一页。
Beckman Coulter AU分析器的Prealbumin测定系统手册说明书
B AOSR6x75.01 OSR Special Chemistry 2009-08 PREALBUMINOSR6175 4 x 15 mL R1 4 x 6.5 mL R2Intended UseSystem reagent for the quantitative determination of Prealbumin (PALB) in human serum on Beckman Coulter AU analyzers.SummaryPrealbumin is a transport protein. It plays a significant role in the metabolism of vitamin A by complexing with retinol-binding protein which in turn complexes with Vitamin A transporting it through the body. This protein is an acute phase reactant whose levels fall in inflammation, malignancy, cirrhosis of the liver and protein wasting diseases of the gut or kidneys. Decreases are associated with liver disease and malnutrition. Levels of Prealbumin increase in Hodgkins disease.1,2MethodologyImmune complexes formed in solution scatter light in proportion to their size, shape and concentration. Turbidimeters measure the reduction of incident light due to reflection, absorption, or scatter.In the procedure, the measurement of the decrease in light transmitted (increase in absorbance) through particles suspended in solution as a result of complexes formed during the antigen-antibody reaction, is the basis of this assay.System Information For AU400/400e/480, AU600/640/640e/680, AU2700/5400 Beckman Coulter Analyzers. ReagentsFinal concentration of reactive ingredients:Solution of Polymers in Phosphate Buffered Saline (pH 7.1 – 7.3)Rabbit anti-human Prealbumin antiserumAlso contains preservatives.Precautions1. For in vitro diagnostic use.2. Do not ingest. Harmful if swallowed.3. Contains sodium azide as a preservative which may react with lead joints in copper plumbing to form explosive compounds. Even though thereagent contains minute quantities of sodium azide, drains should be well flushed with water when discarding the reagent.Preparation of reagentsThe Prealbumin reagent is ready for use. No preparation is required.Storage and stability1. The unopened reagents are stable until the expiration date printed on the label when stored at 2 - 8°C.2. Opened bottles of reagent are stable for 90 days when stored in the refrigerated compartment of the analyzer.Indications of DeteriorationVisible signs of microbial growth, turbidity, precipitate, or change in color in the Prealbumin reagents may indicate degradation and warrant discontinuation of use.Specimen Collection and PreparationFasting serum specimen, free from hemolysis, is the recommended specimen. Avoid highly lipemic samples, which may produce excessively high scatter signals.3Sample Storage and Stability Serum samples are stable 7 days when stored 2 - 8°C. These samples can be stored frozen (≤ -20°C ) for up to 2 months.Interfering Substances Results of studies conducted 4 show that the following substances may interfere with this Prealbumin procedure:The criteria for no significant interference is recovery within 10% of the initial value.Ascorbate: No significant interference up to 20 mg/dL AscorbateBilirubin: No significant interference up to 40 mg/dL BilirubinHemolysis: No significant interference up to 500 mg/dL HemolysateLipemia: No significant interference up to 500 mg/dL Intralipid** Intralipid, manufactured by KabiVitrium Inc., is a 20% IV fat emulsion used to emulate extremely turbid samples.The information presented is based on results from Beckman Coulter studies and is current at the date of publication. Beckman Coulter Inc., makes no representation about the completeness or accuracy of results generated by future studies. For further information on interfering substances, refer to Young 5 for a compilation of reported interferences with this test.ProcedureA complete list of test parameters and operational procedure can be found in the User’s Guide appropriate to the analyzer.Materials ProvidedPrealbumin ReagentMaterials required but not providedPrealbumin Calibrator (Cat # ODR3029)PrealbuminB AOSR6x75.01 OSR Special Chemistry2009-08 Stability of Final Reaction Mixture The Beckman Coulter AU analyzers automatically compute every determination at the same time interval.CalibrationThe frequency of calibration for the Prealbumin turbidimetric procedure is every 90 days. Calibration of this Prealbumin procedure is accomplished by use of the Prealbumin Calibrator (Cat # ODR3029), which is traceable to IFCC International Reference Preparation CRM470 (RPPHS).Recalibration of this test is required when any of these conditions exist:1. A reagent lot number has changed or there is an observed shift in control values.2. Major preventative maintenance was performed on the analyzer.3. A critical part was replaced.Quality ControlDuring operation of the Beckman Coulter AU analyzer at least two levels of immunology control material should be tested a minimum of once a day. In addition, these controls should be performed after calibration, with each new lot of reagent, and after specific maintenance or troubleshooting steps described in the appropriate User’s Guide. Quality control testing should be performed in accordance with regulatory requirements and each laboratory’s standard procedure.Please note that recovery of Non-Beckman Coulter controls may vary with reagent lots of immunoassay products, due to the use of non-human materials in the controls.Results:Automatically printed out for each sample in mg/dL at 37°C.Dynamic RangeThe Prealbumin turbidimetric procedure is linear from 3 - 80 mg/dL. Samples exceeding the upper limit of linearity should be diluted and repeated. The sample may be diluted, repeated and multiplied by the dilution factor automatically utilizing the AUTO REPEAT RUN.Expected ValuesAdults:617 – 34 mg/dLExpected values may vary with age, sex, diet and geographical location. Each laboratory should determine its own expected values as dictated by good laboratory practice.Specific Performance CharacteristicsThe following data was obtained using the Prealbumin reagent on Beckman Coulter AU Analyzers according to established procedures. Results obtained in individual laboratories may differ.Precision 8Estimates of precision, based on CLSI recommendations,7 are consistent with typical performance. The within run precision is less than 5% CV and total precision is less than 10% CV. Assays of serum pools and control sera were performed and the data reduced following CLSI guidelines above.N = 100 Within run TotalMean, mg/dL SD CV% SD CV%14.1 0.09 0.6 0.20 1.525.3 0.14 0.6 0.29 1.135.5 0.35 1.0 0.42 1.2Method Comparison 8Patient samples were used to compare this Prealbumin Reagent. The table below demonstrates representative performance on AU analyzers. Y Method AU640X MethodAU600Slope 1.028Intercept -0.66Correlation Coeff. (r) 0.999No. of Samples (n) 158Range (mg/dL) 5-75References1. Tietz N.W., Textbook of Clinical Chemistry,Second Edition, Burtis, C.A., and Ashwood E.R., eds. W.B. Saunders Company, 1994.2. Kaplan L.A. and Pesce A.J., Clinical Chemistry Theory, Analysis, Correlation Third Edition, Mosby, St. Louis, Missouri, 1996.3. Rose, N.R., Friedman, H, and Fahey, J.L, Manual of Clinical Laboratory Immunology, Third Edition, American Society for Microbiology, Washington, DC,1986.4. CLSI/NCCLS, Interference Test in Clinical Chemistry, EP7-P, 1986.5. Young, D.S., Effects of Drugs on Clinical Laboratory Tests, AACC Press, 5th Edition 2000.6. Beckman Coulter Inc. data on samples collected from 200 blood donors in North Texas.7. CLSI/NCCLS Evaluation Protocol EP5-T2, 1992.8. Data is on file for specific AU analyzersManufactured by: Beckman Coulter, Inc., 250 S. Kraemer Blvd. Brea, CA 92821, USA。
美国PerkinElmer公司AAS石墨炉操作手册
美国PerkinElmer公司AAnalyst系列AAS石墨炉操作手册珀金埃尔默仪器（上海）有限公司姚继军编译张扬祖审校安全信息前言和分析仪器配套的这本手册中包含一些辅助信息和注意事项，请用户遵守这些注意事项，以保证安全操作和仪器的安全使用。
这些注意事项是以遵守国家安全行为标准为前提的，它只是国家安全行为标准的补充。
有关原子光谱的安全操作和各种原子吸收技术的潜在危险已经在原子吸收光谱仪的用户手册中介绍过，故在使用本仪器之前请阅读原子吸收光谱仪的用户手册。
该手册中提到的注意事项并不能完全涵盖实际使用中的所有安全规范。
一个安全的实验环境从根本上是要靠用户和用户所在的单位来维护的。
分析仪器的正确使用为了得到更好的效果，在安装和使用仪器之前，应该熟悉系统中所有的仪器，并且知道怎样操作它们。
首先应该了解你所在实验室的安全规范，特别对于那些原子光谱仪器的安全规范更应该了解。
在操作仪器以前请先阅读与仪器配套的用户手册。
如果没有按用户手册中说明的方法操作仪器，或者使用作用户手册中没有提及的用途，可能会造成仪器的损坏，或者危及你自己和其他人的安全。
只有经过资格认证或者经过充分培训的人员才能操作仪器。
石墨炉分析的准备工作原子化室门升高或降低，按下面的步骤来升高或降低原子化室门抬高或降低原子化室门1) 把左手的手指放在把手后面，用拇指按住弹簧按钮；2) 按住弹簧按钮不放，用双手扶着炉门，可以将原子化室门升高或降低到最上边或最下边的位置。
只要松开弹簧按钮，炉门也可以停留在其他任何位置。
拆卸和重装操作带有自动取样机的石墨炉，必须要卸下原子化室门。
按下边的步骤拆卸和重装原子化室门。
拆卸原子化室门拆卸原子化室门：1.将原子化室门移到最低位置；2.旋出原子化室门的锁紧旋钮；3.小心地拔出左边导轨的两个销钉；4.拔出右边导轨的原子化室门固定条，完成拆卸。
重装原子化室门：1.将原子化室门固定条插入右边导轨的插槽；2.上下移动原子化室门，直到两个销钉对准左边导轨上的洞，将销钉推进洞中；3.旋紧原子化室门的锁紧旋钮，完成重装。
BOSHU手册文字完整版
柏束BOSHU手册1、封面2、法国巴黎铁塔图3、品牌缘承（文字）柏束BOSHU一个专业个人护理及研发美容护肤产品的国际化品牌，前身为风靡欧美地带的一个法国香水品牌PAU，凭借其不断创新的精神与精益求精的追求完美品质的经营理念，1982年在法国诞生FRANCE BOSHU COSMETICS AGENCIES，至今已在法国美容护肤品市场，傲然屹立二十几年，成功的树立高贵典雅的国际化品牌形象，BOSHU在欧美国家已成为一个女性所熟悉的著名品牌。
她来到了China（中国），此刻东方佳人的肌肤新生体验，从拥有柏束BOSHU开始、、、、、、新的体验让生活保持日久长新的感觉，我们的肌肤同样渴求这种感觉，身处繁忙的都市生活中，年龄的增长，睡眠的不足，工作疲劳、空气污染，紫外线照射等各种内外部因素让我们的肌肤不堪重负，肌肤修补能力随之减弱，皱纹、面黄、暗沉、干枯等多种肌肤问题频频出现，当我们为人生的历史弥新喝彩时，也在为肌肤失去光彩而叹息。
肌肤需要新的体验，柏束BOSHU深谙肌肤之道，为不同类型的面部肌肤定制了专业的护理产品，从清洁—爽肤—润肤—日常护理—特殊护理的每一个环节给肌肤最周到细致的呵护，开启肌肤宛如回归大自然重获新生的体验，让岁月的沉淀在肌肤上不着痕迹，重新绽放动人光彩。
美丽并快乐着是新世纪的价值观，美丽的生活从这里开启。
相信美丽，你就会得到美丽的厚爱；追求美丽，你就会得到美丽的眷顾；创造美丽，你就会得到美丽的回报；同样的人生百年，柏束BOSHU会让您活得更年轻。
柏束BOSHU ——每天美一点4、水能量高保湿系列（产品图+以下文字）水乃万物之源，近水心洁，近香心芳，爱美的您是否关注皮肤的干渴？皮肤的营养和水分主要是靠血液在供应，因此疏通面部血管的微循环，内供外补，是保持你皮肤莹润、补水的唯一途径，容用仿生补水，分层瞬透，体验超凡水能量储水功能，同时有效的增加皮肤的吸收能力，补充充足的水分和营养，让您的肌肤从深处荡起如水的波，反射出那份清澈的光泽。
Agilent 7000B手册(合订本)
目录第一章串联四级杆气相质谱仪工作原理 (3)1.1 气相色谱1.2 离子源1.3 四级杆质量分析器1.4 碰撞池1.5 检测器1.6 Masshunter 软件第二章安捷伦7000B 气相串联质谱仪开关机步骤及调谐 (8)2.1 安捷伦7000B气相串联质谱仪配置2.2 质谱仪开机步骤2.3 质谱调谐2.4 质谱仪空气检漏2.5 质谱仪关机步骤第三章串联质谱扫描模式及及数据采集方法编辑运行 (13)3.1 安捷伦串联四级杆可设定的扫描模式3.2 串联质谱运行方法编辑3.2.1 气相配置设定3.2.2 编辑运行方法的气相参数（包含碰撞池气体流量设定）3.2.3 运行方法质谱参数设定3.3 单个质谱方法运行3.4 Sequence 自动进样序列表设定及运行第四章 MRM 方法开发概诉 (24)4.1 多重反应监测（MRM）的详细过程4.2 MRM方法的开发过程4.3 如何使用QQQ方法优化助手第五章定性分析 (27)5.1 了解定性分析的基础知识5.1.1工具栏5.1.2数据文件浏览5.1.3色谱图窗口5.1.4浏览数据点5.1.5获得质谱图5.1.6质谱图扣背景5.1.7方法编辑窗口5.2全扫描数据的定性分析5.2.1积分5.2.2定义色谱图5.2.3 计算信噪比5.2.4查找和识别化合物5.2.5谱库检索5.2.6输出报告5.2.7谱图显示选项第六章定量分析 (39)6.1创建定量的批处理和定量方法6.1.1 新建batch6.1.2向 Batch中引入数据文件6.1.3检查/补充定量数据的信息6.2新建定量方法6.2.1 MRM Compound setup6.2.2 Retention Time Setup6.2.3 ISTD Setup6.2.4 Concentration Setup6.2.5 Qualifier Setup6.2.6 Calibration Curve Setup6.2.7 定量高级功能设定--- 积分参数6.2.8 离群数据范围设置6.2.9 Validate method6.2.10 退出并保存定量方法6.3 数据分析6.3.1 Analyze Batch6.3.2校正曲线的修改6.3.3定量表中的提示符号6.3.4 保存batch6.4 定量报告第一章串联四级杆气相质谱仪工作原理安捷伦串联气相质谱仪由六个部分组成，分别为：1．气相色谱部分2．离子源3．第一极四级杆及第二级四级杆4．碰撞池5．检测器6．Masshunter 软件7890气相色谱仪1.1 气相色谱对于质谱仪来说，气相色谱主要是进样仪器。
USP 34 621 色谱法 中文译稿
<621>色谱法介绍色谱分离技术是通过样品组分在固定相和流动相两相中的分布差异进行分离的技术。
其中固定相可以是固体、有固相支持的液体或凝胶。
固定相可以填充于柱、分散成层、分布为膜或者应用于其他技术中。
流动相可以为气态、液态或超临界流体。
分离可以基于吸附性、质量分布（分配）或离子交换，也可以基于分子物理化学性质的差异，如大小、质量和体积。
本章节包括了基本步骤、定义和对一般参数的计算并描述了对于系统适应性的基本要求。
在USP中应用于定量和定性分析的色谱方法类型有柱色谱法、气象色谱法、纸色谱法、薄层色谱法（包括高效薄层色谱）和加压液相色谱法（一般称作高压或高效液相色谱）。
基本步骤本部分描述了使用某种色谱方法的基本步骤。
除另有各论规定外，以下色谱分离方法的步骤将会被遵循。
纸色谱法固定相：固定相为一张适当质地和厚度的纸。
色谱图的形成过程可以是上行的，这样溶剂被毛细管作用力支撑着沿着纸向上，这个过程也可以是下行的，在此情况下溶剂流动也受到重力的影响。
与溶剂流动有关的纸张纹理定向应该在一系列色谱图中保持恒定。
（纤维方向通常由制造商在色谱纸的包装上标出。
）仪器：纸色谱法的必备仪器包括装有添加溶剂的入口的气密室和短于该室内部高度5cm的耐腐蚀材料支架。
该支架作为用于溶剂槽以及用于抗虹吸棒的支撑，这些抗虹吸棒依次撑起色谱纸。
气密室的底部以规定的容积系统或流动相覆盖。
使用以规定溶剂系统润湿的纸张衬托于气密室的内壁，以增加气密室的溶剂蒸汽饱和度。
斑点：将待分析的一个或多个物质溶解于适当溶剂中。
以微量吸管吸取适当体积的溶液，其中通常含有1-20µg 该化合物，点样为6-10mm大小斑点且斑点间的间隔不小于3cm。
下行色谱法步骤1.带斑点的色谱纸以抗虹吸棒悬挂在气密室内，该棒将该色谱纸的上端固定在溶剂槽中。
（注：确保色谱纸挂在抗虹吸棒下的部分自由的悬挂在气密室中，没有接触到支架、室壁或室内的液体。
2.气密室被密闭，以便使该室与色谱纸达到溶剂蒸汽平衡（饱和）释放任何多余压力。
Polish Tube-NaCl MgSO4 50 PK Part Number 5982-0101
Polish Tube-NaCl/MgSO4, 50/PK, Part Number 5982-0101*************(24小时)化学品安全技术说明书GHS product identifier 应急咨询电话（带值班时间）::供应商/ 制造商:安捷伦科技贸易（上海）有限公司中国（上海）外高桥自由贸易试验区英伦路412号（邮编:200131)电话号码： 800-820-3278传真号码: 0086 (21) 5048 2818Polish Tube-NaCl/MgSO4, 50/PK, Part Number 5982-0101化学品的推荐用途和限制用途5982-0101部件号:物质用途:供分析化学实验室使用的试剂和标准50 x 15 ml（毫升） , 2 g / 管安全技术说明书根据 GB/ T 16483-2008 和 GB/ T 17519-2013GHS化学品标识:抛光管-NaCl/MgSO4，50/PK，部件号 5982-0101有关环境保护措施，请参阅第 12 节。
物质或混合物的分类根据 GB13690-2009 和 GB30000-2013紧急情况概述固体。
白色。
/ 白色。
无气味的。
操作和/或处理此物质可能产生能够导致眼睛，皮肤，鼻腔和喉部机械刺激的粉尘。
物理状态:颜色:气味:GHS危险性类别警示词:警告危险性说明::防范说明预防措施:事故响应:便地取出，取出隐形眼镜。
继续冲洗。
P337 + P313 - 如仍觉眼刺激： 求医要么就诊。
安全储存:不适用。
废弃处置:不适用。
标签要素象形图皮肤腐蚀/刺激 - 类别 3严重眼损伤/眼刺激 - 类别 2A物理和化学危险没有明显的已知作用或严重危险。
健康危害::与物理,化学和毒理特性有关的症状皮肤接触食入吸入不利症状可能包括如下情况：呼吸道疼痛咳嗽没有具体数据。
不利症状可能包括如下情况：刺激充血发红:::眼睛接触:不利症状可能包括如下情况：疼痛或刺激流泪充血发红延迟和即时影响，以及短期和长期接触引起的慢性影响短期暴露潜在的即时效应:无资料。
美国LABCONCO超纯水-中文资料
WaterPro PS 化学通用型纯水工作站，220V，带出水枪
WaterPro PS/HPLC 纯水工作站，220V
WaterPro PS/HPLC 纯水工作站，220V，带出水枪
WaterPro PS/UF 纯水工作站，220V
WaterPro PS/UF 纯水工作站，220V，带出水枪
WaterPro PS HPLC/UF 复合型纯水工作站，220V，带出水枪
超纯水系统
WaterProTM 纯水系统
实验用水要求相当高，普通的自来水无法满足要求。纯水系统采用一种或多种纯化方式使普通水纯化为纯水或 超纯水。
WaterProTM PS 超纯水工作站
● 生产实验室所需的 I 类纯净水，电阻率最高可达 18.2MΩ-cm，并有 LED 显 示，可适于不同分析之需要
● 最大出水率为 1.8L/ 分钟 ● 304 型不锈钢外壳，有良好的抗腐蚀性 ● In-Line 压力调节器，进水压力范围：0~100psi，有效防止过高水压对仪器
造成损害 ● 1/4HP 马达和循环泵，可自动进水，补水及自循环 ● 定时、定量取水，自动控制 ● 在线水温检测及显示 ● 定时启动自动循环，防止关机状态下的微生物滋生 ● 超大、高效、分立式滤芯保证高通量、长寿命，同时降低运行成本 ● 出水枪使操作更方便灵活，并可实现出水量以“滴”为计量单位 ● 采用不同的水纯化技术，可以形成不同的 WaterPro PS 工作站 ● 除化学通用型之外，其余均有双波长紫外氧化灭菌功能 ● 每种型号均有台式或壁挂式可选
化学通用型 /UF 型套柱，适用于 90005-02，-03 和 90007-02, -03 适用, 包括活性碳滤芯(1)，去离子滤芯(3) HPLC 型 / 复合型套柱,适用于 90006-02，-03 及 90007-05，包括活性碳滤芯(1)， 去离子滤芯(2),有机吸附滤芯(1)
BECODISC深层过滤板产品数据表（第1页）说明书
技术数据表深层过滤BECODISC® BP 系列用于制药行业的碟片式滤芯BECODISC BP 碟片式滤芯符合制药行业的高要求。
BECODISC BP 碟片式滤芯所采用的超纯原材料和特殊生产工艺，使其具有内毒素含量低的特点。
该系列产品能够在多种药品的过滤过程中高效截留内毒素。
BECODISC BP 碟片式滤芯的具体优势：-高内毒素截留率以及卓越的细菌截留率。
-这种创新的生产工艺可保证内毒素含量小于0.125 EU/ml。
-最大原材料纯度和最小可溶性离子迁移-将各种过滤机制（表面、吸附、深层过滤）和吸附性能完美结合，可确保最大的可靠性。
-面向所有原材料和辅助材料的综合质量保证以及严格的过程控制可确保成品质量一致。
-在交付之前，对 BECODISC BP 碟片式滤芯进行LAL 测试，确保热原含量 < 0.125 EU/ml。
可应要求提供证书。
-可提供完整性验证指南。
减少和去除微生物BECODISC B01P、B02P、B04PBECODISC 碟片式滤芯具有密孔结构和电势吸附可实现较高的微生物截留率。
这些碟片式滤芯具有高内毒素截留率的特性。
由于对胶体类物质的出色截留能力，这些过滤板特别适合用作后续膜过滤的预滤器。
精细过滤BECODISC B08P用于实现高澄清度的 BECODISC 碟片式滤芯。
这些碟片式滤芯可靠地截留超细颗粒并降低生物负载。
在实际应用中，这些深层过滤板是保护膜滤器、反渗透系统，和保护色谱柱的理想预滤器。
澄清过滤和粗滤BECODISC B20P、B40P具有大容量孔隙结构的 BECODISC 碟片式滤芯。
这些碟片式滤芯具有高颗粒截留能力，非常适合澄清过滤应用。
物理数据此信息旨在作为选择 BECODISC 碟片式滤芯的指南。
透水性是一个实验室值，表征不同的 BECO 深层过滤板。
并非是建议工艺流速。
类型* 所使用的 BECO ® 深层过滤板标称截留率厚度 含灰量 湿破裂强度 透水性 内毒素含量***μm mm % kPa** Δ p = 100 kPa**l/m 2/minEU/ml B01P PR Steril S100 0.1 3.9 58 > 50 30 < 0.125 B02P PR Steril S80 0.2 3.9 50 > 80 46 < 0.125 B04P PR Steril 40 0.4 3.9 49 > 50 61 < 0.125 B08P PR 12 0.8 3.9 50 > 130 175 < 0.125 B20P PR 5 2.0 3.9 50 > 60 330 < 0.125 B40PPR 14.04.348> 452381< 0.125* B = 聚丙烯封装（例如 B01P ） ** 100 kPa = 1 bar*** 用50 l/m ² WFI （注射用水）冲洗后分析内毒素含量订购信息1 扁平适配器 / 双 O 形圈适配器 |2 带限位隔轨 |3 不能与双 O 形圈适配器搭配例如：B01P62SF带 BECO PR Steril S100 深层过滤板的聚丙烯碟片式滤芯，标称截留率为 0.1 µm ，16 个滤囊，276 mm 高， 12"，具有硅橡胶垫圈和扁平适配器。
VW、NASM、DVS等国外标准译文
其它国外标准译文ENG-STND-0005 液体涂料涂装件外观规范ENG-STND-0007 高压压铸铝件及机加工件标准ENG-STND-0011 管材和平轧材标准ENG-STND-0018 粉末涂料涂装件外观规范ENG-STND-0067 电泳涂装件外观标准PRCI IM-2-1 设施完整性管理程序指南NEMA ICS 8-2011 工业控制和系统起重机控制器NEMA SM 23-1991(R2002) 机械驱动用汽轮机SAA HB 59-1994 人体工程学—人为因素工作系统设计实用方法WRC BUL 275-1982 淬火加回火2 1/4Cr-1Mo钢在炼油工艺中厚壁反应器容器上的使用：25年研究和应用的解释性评论WRC BUL 305-1985 公报305AAR：2017 标准与推荐做法手册AD 2000-MERKBLATT W0-2016 压力容器用材料材料的通用原则AD 2000-MERKBLATT A4-2015 压力容器的设备、安装和标记附件外壳AD 2000-Merkblatt W5-2009 压力容器用材料铸钢AD 2000-MERKBLATTW10-2016 压力容器用材料低温黑色金属材料ASABE EP369.1-1987（R2014）农业排水泵站的设计CCH 70-4-2014 水利机械用钢铸件技术规范CSA 3.16-2015 杠杆操纵的非润滑型燃气切断阀ETS-0967 金属涂层技术ETS-1083_R01 紧固件—T1螺栓连接副F69A4_S1 锌和铝基无机防腐蚀涂层美国3D打印标准化路线图增材制造标准化路线图AAR M-214-2009 已用过和翻修侧架和摇枕—分类和维修程序AAR M-300-2004 翻修制动梁AAR M-1002-R-2014 罐车罐体的维修、改良和改装AAR S-2044-2016 货车的安全器械要求ASCE 管道复原系统设计的新兴概念US EPA 8270D-2014 气质联用仪测试半挥发性有机化合物AC 20-107B-2009 飞机复合材料结构cyber vision2025-afd-130327-306 美国空军赛博空间科学与技术愿景 2012-2025 ANSI/EIA-364-01B-2000(R2012) 电连接器的加速度试验程序ANSI/EIA-364-02D-2012 电连接器的空气泄漏试验程序ANSI/EIA-364-03C-2009 电连接器的低气压浸渍试验程序ANSI/EIA-364-05B-1998(R2009) 电连接器的接触件插入力、松开力和拔出力试验程序ANSI/EIA-364-06C-2006(R2012) 电连接器的接触电阻试验程序ANSI/EIA-364-07C-2007(R2012) 电连接器的接触件同轴度试验程序ANSI/EIA-364-09C-1999(R2012) 电连接器和插座的耐久性试验程序ANSI/EIA-364-11C-2014 电连接器和插座的耐溶剂性试验程序ANSI/EIA-364-14B-1999(R2012) 电连接器的臭氧暴露试验程序ANSI/EIA-364-22B-2000(R2012) 模拟条件下的电连接器使用寿命试验程序ANSI/EIA-364-24B-1998(R2009) 电连接器的维修老化试验程序ANSI/EIA-364-25D-2010 电连接器的探针损伤试验程序ANSI/EIA-364-27C-2011 电连接器和插座的机械冲击(规定脉冲)试验程序ANSI/EIA-364-29C-2006(R2013) 电连接器的接触件固定性试验程序ANSI/EIA-364-32G-2014 电连接器和插座的热冲击(温度循环)试验程序ANSI/EIA-364-35C-2012 电连接器的绝缘安装板固定性试验程序ANSI/EIA-364-38D-2014 电连接器的电缆拉脱试验程序ANSI/EIA-364-39B-1999(R2013) 电气连接器、触点和插座的静水压测试程序ANSI/EIA-364-40B-1998(R2009) 电气连接器的挤压测试程序ANSI/EIA-364-41E-2010 电气连接器的电缆挠性测试程序ANSI/EIA-364-42C-2012 电气连接器的冲击测试程序ANSI/EIA-364-45C-2012 电气连接器的防火墙火焰测试程序ANSI/EIA-364-46C-2012 电子连接器、电接触元件及插座的微秒间断试验规程ANSI/EIA-364-53B-2000(R2016) 电气连接器和插座的硝酸蒸汽测试、镀金制品测试程序ANSI/EIA-364-54A-1999(R2012) 电气连接器、触点和插座的磁导率测试程序ANSI/EIA-364-56E-2011 电气连接器和插座的焊锡耐热性测试程序ANSI/EIA-364-66A-2000(R2013) 电气连接器EMI屏蔽效能测试程序ANSI/EIA-364-71C-2008(R2014) 电气连接器和插座的焊料芯吸（波峰焊接技术）测试程序ANSI/EIA-364-88-1995(R2009) 电子连接器的剩磁ANSI/EIA-364-104A-2000(R2008) 电气连接器的易燃性测试程序ANSI/EIA-364-105-B-2015 电气连接器和插座的高压低温测试程序ANSI/EIA-364-106-2000(R2013) 电气连接器的驻波比 (SWR) 测试程序ANSI/EIA-364-110-2006(R2013) 电子连接器和插座的热循环试验规程EIA-364-1000-2008 评估受控环境应用中电连接器和插座性能的环境测试方法IATF 16949-2016 汽车生产件及相关服务件组织的质量管理体系要求NAS 4003-2012 A286高温合金外螺纹紧固件，极限抗拉强度为160 KSI，极限抗剪强度为95KSI，1000℉NASM 1312-1-2010(R2014) 紧固件试验方法方法1—盐雾NASM 1312-4-2011 紧固件试验方法方法4—搭接接头的抗剪NASM 1312-7-2012 紧固件试验方法方法7—振动NASM 1312-11-2013 紧固件试验方法方法11—抗拉疲劳NASM 1312-13-2013 紧固件试验方法方法13—双剪试验NASM 1312-15-2012 紧固件试验方法方法15—力矩-拉力NASM 1312-18-2012 紧固件试验方法方法18—高温抗拉强度NASM 1312-19-2012 紧固件试验方法方法19—紧固件的密封NASM 1312-24-2012 紧固件试验方法方法24—托板紧固件的壳体拧脱NASM 1312-25-2012 紧固件试验方法方法25—扳拧槽力矩质量一致性试验NASM 1312-30-1997 紧固件试验方法方法30—抽芯铆钉的板拔出NASM 1312-31-2011 紧固件试验方法方法31—力矩DVS 1608-2011 铁路应用中铝合金焊接结构的设计及强度评价VDA 239-200-2013 铝薄板材料TSI 2014-32-EU-2015 关于各成员国市场上销售的计量器具的协调法律(改写)FM 1042-2016 叶片式水流报警指示器认证标准FM 1626-2011 立管管汇总成认证标准FM 3132-1970 压力致动水流开关认证标准AATCC 100-2012 纺织材料抗菌整理剂的评价AIA-NAS NAS 578-2012 浮动桶形螺母用支架驾驶舱内移动设备集成：优势、挑战和建议RTCA-DO-355-2014 持续适航信息安全指南TL 203-2015 金属部件上装饰性镀铬层（Ni–Cr镀层）表面防护要求航空赛博安全——寻找升力，减少阻力CAN/ULC-S548-15 水式灭火系统用装置和附件标准VW 01054: 2016 图纸尺寸标注和公差标注—包容要求和独立性原则VW 01088-2004 工件边缘—定义，图纸技术规范VW 13750-2016 金属零件的表面防护—表面防护类型，代码VW 50180-2015 车辆内部部件—散发性能VW 50185-2016 车辆零件—耐露天气候老化性QQ：416711838。
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纯Nafion®干燥管是最佳的选择。它的一体化结构没有可拆卸的零部件，无需维护。而且在不影响待
分析物的情况下能够连续且高选择性的以气态形式去除水份，经Nafion®干燥管处理后的样气出口露
点最低可达-45℃。
燃料电池加湿
某些类型的燃料电池需要对氢气和氧气流进行加湿以增加效能。虽然现存有很多技术能够加湿气
博纯的FC™系列加湿器符合行业标准，能提供无与伦比的稳定性和可靠 性，并具有很长的使用寿命。旨在满足用户对燃料电池的严格要求，FC 系列产品能为指定流量范围内的空气和氢气提供可持续且重复的加湿。 博纯加湿器特性为低压降，运行不需电力，大大减少系统的实际负载。 FC™系列具有坚固的可定制的外壳，以满足不同工况要求。FC™系列 加湿器是便携式、固定式、材料处理汽车和不间断电源等应用的良好选 择。在某些情况下，其运行寿命高达20,000小时。
气－气加湿模式采用反向流动的干湿气流，在运行中水份发 生交换。这种运行的能效很高，并不需要额外的加热。气－ 气加湿模式有热交换的功能，可将湿气流中的大部分热量转 移到干燥的气流中。博纯大部分的加湿器都具有水-气及气-气 增湿功能（FC-100除外）。
湿度、压力和化学特性
Nafion®管在160℃时，化学性质依然稳定，且能够承受超过 8 0 p s i g 的 压 力 。 和 Te f l o n 一 样 ， 它 的 化 学 惰 性 非 常 强 ， 能 够 抵抗绝大多数化学物质的侵蚀。即使在高温下也能抵御高浓 度的腐蚀性气体如HCl、H2S和HF等。
5
Nafion® 优势
优势
● 和其他技术相比，博纯干燥器和加湿器对水份具有相当高的选择性 ● 在干燥过程中，可有选择性的完整保留工艺样气中的待测气体 ● 样气能够干燥至露点－45℃或加湿至100％RH。 ● 水份的转移在若干分之一秒内即完成 ● 整个运行过程连续且自我再生 ● 整套设备结构紧凑，牢固且具有极强的耐腐蚀性 ● 无活动部件，免日常维护 ● 干燥及加湿过程中无需使用电源，可适用于高防爆等级的危险区域
博纯加湿器既可以进行水－气增湿，也可以进行气－气增湿。 当进行水－气增湿时，水在干燥管外侧运行，样气在管内被 加湿。该种加湿方法能够产生最大的湿度，因为和水接触的 Nafion®管壁的磺酸基一直处于饱和状态，在此种加湿方法中， 可以用热水来增加加湿的效果。水从液相转为气相的过程中， 因为需要消耗能量，干燥管会自动降温而轻微地降低样气的湿 度，若不使用热水，会轻微降低水份交换的效率。
Richard Curran 博纯总裁
3
Nafion®简介
最佳的水份交换材料
耐 腐 蚀 — N a f i o n ®是 聚 四 氟 乙 烯 [ Te f l o n ®] 和 全 氟 - 3 ， 6 - 二 环 氧 - 4 - 甲 基 - 7 - 癸 烯 - 硫 酸 的 共 聚 物 ， 象 Te f l o n 一 样 ， N a f i o n ®具 有 极强的抗化学侵蚀特性，所以它能被用于强酸性气体的场合。
我们对中国市场有着很高的期许，同时也将逐步加大投资力 度，接下来我们将在上海建立客户支持、服务中心，这也是我 此行的目的之一。另外，我们非常高兴和欣慰的是，我们已经 在中国寻求找到了一些很好的合作伙伴，以刚刚结束 的万众瞩 目的北京奥运会为例，众所周知，赛默飞世尔公司是北京环境 监测领域的主要供应商，而我们也很荣幸地与赛默飞世尔达成 合作，在空气中的氮氧化物检测中，提供Nafion®干燥管进行样 气的干燥。当然，北京奥运会对于赛默飞世尔和博纯来说只是 一次很好的发展契机，而中国政府和人民对环境治理的深入理 解和渴望，都将对中国的环境监测带来深远的影响，这对于仪 器供应商来说也意味着巨大的市场潜力。
博纯 创新的样气预处理技术领导者
Perma Pure,the leader in Gas Conditioning
美国博纯简介 Perma Pure Profile
创新的样气预处理技术领导者
美国博纯有限责任公司（Perma Pure LLC）总部设在美国新 泽西州Toms River，是豪迈集团 (Halma p.l.c.) 旗下的子公 司。我们是气体采样和预处理类产品如，干燥器、加湿器、 过滤器、冷凝器、特种气体洗涤器及完整采样系统的世界顶 级制造商。长期以来公司运用Nafion®膜渗透技术，连同其 它多样技术和专业知识，帮助客户安全、准确地分析采样气 体。现公司面向全球的医疗、燃料电池、工业及科学应用领 域提供相关样气预处理系列产品。在医疗上的应用包括麻醉 检测、呼吸监测及代谢测试中对呼吸气体进行干燥，同时对 呼吸器的供气或供氧进行加湿。工业应用主要在过程分析和 环保监测中的气体采样预处理。燃料电池和科学应用主要是 燃料电池加湿。同时还可应用于实验室的气体分析采样预处 理。1992年，英国投资集团Halma将博纯公司纳入旗下，随 后公司成功收购BALDWIN品牌，产品体系中增加了冷凝器、 采样探头、过滤器等针对工业领域应用的产品，从而转变成 为气体分析预处理领域的行业整体解决方案供应商。2013 年初公司荣获ISO13485:2003医疗设备生产质量体系认证， 这是博纯在原有ISO 9001:2008之上对质量认证的又一次扩 展。目前，随着业务的拓展，我们正着力于成为全球范围内 完善的工程设计、制造及服务供应商。
完全保留
大气气体
碳氢化合物
N2 O2 H2 Ar He 氧化物
所有简单碳氢化合物 有毒气体
CO CO2 SO2 SO3 NOX 卤素
HCN COCI2 NOCI 其他有机物
CI2 F2 HCI HF HBr 氟碳化合物 含硫化合物
醚 氰化物 酯 无机酸
H2S COS 硫醇
HNO3 H2SO4
部分流失
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干燥器和加湿器工作原理
干燥原理
Nafion®加湿器
当气体通过Nafion®干燥管的时候，水份被管道内壁吸收并且通 过外壁渗出。除水的过程是靠管道内外的湿度差产生的，样气 中的水份在不到1秒钟的时间内就会从管内转移到管外。
大多数的博纯干燥器和加湿器内装有一根或多根Nafion®干燥 管并有一个外壳供吹扫气反向流动，这种管壳式的设计已被 证实其对于水份的转化十分有效。
除了Nafion®干燥管，博纯干燥管和加湿器还包括外壳和相应 的接头，在多管束系列中还使用了环氧树脂的连接头。单根 Nafion®管的干燥器和加湿器能够适应于任何接头。多管系列 的干燥管因为使用了环氧类的接头，在某种程度上惰性要差 一些。外壳和接头的材料可选用不锈钢，氟碳聚合物以及聚 丙烯等不同材质。
干燥器和加湿器的耐温性能取决于其制作材料，聚丙烯材料 最高可以耐温100℃，氟碳为150℃，不锈钢为160℃。若使 用多管系列，因为环氯树脂的原因，最高温度为150℃。若无 强化处理所有干燥管和加湿器的最大承受压力为80psig。具 体温度和压力请联系博纯销售代表。
吹扫气出口
样气进口
样气出口
吹扫气进口 干燥器和加湿器工作原理
快速 — 因为含有磺酸基团，Nafion®具有极强的渗水性。在此 化学结构中，磺酸基最多可以接受13个水份子。通过磺酸基 团，在Nafion®管壁上形成了一个交联的离子通道，水在管壁表 面经过磺酸基吸收后，通过离子通道迅速地转移至管壁的另一 面，然后蒸发。
选择性 — 与微孔渗透膜是一种相对较慢的扩散过程不同， Nafion®对水份的吸收和转移是非常迅速的水合过程。这是一个 只和水发生的特殊化学反应，其他物质通常不会受到影响。
过程简单 — 当水份在气相的状态下由管内转移到管外，没有自 由能的变化，所以不需要额外的能量来驱动该反应。反应的驱 动力来源于管内和管外的水份浓度差（湿度差）。
- [ (CF2 - CF2)m - CF - CF2]n -
When m=5 to 13.5 n=ca.1,000 z=1,2,3... x=1 to 13
医疗 燃料电池 科学研究
呼吸气体分析中最为常见的问题是采样中的水汽。它可导致采样管道和测 量元件内的冷凝水从而对二氧化碳监控（IR）产生干扰。博纯ME™系列 水份交换器有选择性的只去除采样中的水蒸气，从根本上消除分析仪的失 效根源。博纯供应各类直径、长度和配合转接头的干燥管，ME™系列应 用广泛，适合不同流速范围。
应
体，但要实现精确的，连续的且低成本的加湿并不容易。焓轮加湿技术不仅耗能，而且存在密封问
用
题，一旦设备进水就会失效。超声波设备易堵塞设备而且必须对气体流量进行匹配控制比较困难。
博纯的气体加湿器是最佳选择。它可以持续不断地加湿气流，没有可拆分的零部件，而且不需要耗 能。它们可以在很宽泛的工况下运行，且可得到持续稳定的加湿效果。
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O
|
CF2
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CF - CF3
|
Z
O
|
CF2
|
CF2
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SO3H ● [H2O]X
Nafion®化学结构示意图
样气干燥
样气分析需要保证其干燥、洁净，才能确保分析结果的精确和可靠。过滤器能够除去颗粒物，但是
应
从样气中除去水份并且不影响待分析物则并不容易。冷凝器（包括帕尔帖冷凝器）适于冷凝除去水
用
份，但易溶于水的气体成份同时也会因此流失。干燥剂能吸收水份，但也会吸收待分析物。美国博
ME™－系列加湿器由Nafion®管组成但是受到聚丙烯编织套 的保护。当气体通过Nafion®管的时候，气体湿度和环境湿度 达到平衡。这些加湿器既可以用于干燥也可以用于增加样气 湿度。
Nafion®干燥管
博纯干燥管中，干燥的吹扫气持续通过Nafion®管的外表面， 从干燥管内的气流中带走水蒸气，使样气得到干燥且不会产 生冷凝水以致待分析物溶于水而损失。
极性有机物
醇，酮，有机酸， 二甲基亚砜，醛 四氢呋喃
其他 氨，胺，腈
警告：氨气会对Nafion®管造成不可逆的损坏，请注意！在样 气中存在氨气的情况下，建议使用除氨器。