Thiophilic adsorption revisited
Specific and efficient selection of serum immunoglobulins, but not other proteins, on T-gel remains difficult. T-gel capacity was determined for different activation conditions and serum loadings. Mass spectrometry analysis was used to identify the proteins found in the flow-through and in the elute...
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Veröffentlicht in: | Journal of chromatography. B 2007-01, Vol.845 (2), p.226-231 |
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container_title | Journal of chromatography. B |
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creator | Hardouin, Julie Duchateau, Magalie Canelle, Ludovic Vlieghe, Céline Joubert-Caron, Raymonde Caron, Michel |
description | Specific and efficient selection of serum immunoglobulins, but not other proteins, on T-gel remains difficult. T-gel capacity was determined for different activation conditions and serum loadings. Mass spectrometry analysis was used to identify the proteins found in the flow-through and in the eluted fractions. Alpha-2-macroglobulin and albumin were the major contaminants of the eluates. The influence of the competition between immunoglobulins and the other serum proteins on the adsorption was also studied. Using a serum depleted in immunoglobulins (flow-through of a first chromatography on T-gel), many serum proteins were retained on the T-gel, including albumin. We conclude that T-gel selectivity is less than absolute and may reflect for a large part the experimental conditions of the adsorption. |
doi_str_mv | 10.1016/j.jchromb.2006.08.017 |
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T-gel capacity was determined for different activation conditions and serum loadings. Mass spectrometry analysis was used to identify the proteins found in the flow-through and in the eluted fractions. Alpha-2-macroglobulin and albumin were the major contaminants of the eluates. The influence of the competition between immunoglobulins and the other serum proteins on the adsorption was also studied. Using a serum depleted in immunoglobulins (flow-through of a first chromatography on T-gel), many serum proteins were retained on the T-gel, including albumin. 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B</title><addtitle>J Chromatogr B Analyt Technol Biomed Life Sci</addtitle><description>Specific and efficient selection of serum immunoglobulins, but not other proteins, on T-gel remains difficult. T-gel capacity was determined for different activation conditions and serum loadings. Mass spectrometry analysis was used to identify the proteins found in the flow-through and in the eluted fractions. Alpha-2-macroglobulin and albumin were the major contaminants of the eluates. The influence of the competition between immunoglobulins and the other serum proteins on the adsorption was also studied. Using a serum depleted in immunoglobulins (flow-through of a first chromatography on T-gel), many serum proteins were retained on the T-gel, including albumin. We conclude that T-gel selectivity is less than absolute and may reflect for a large part the experimental conditions of the adsorption.</description><subject>Adsorption</subject><subject>Analysis</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological and medical sciences</subject><subject>Chromatography, Liquid</subject><subject>Chromatography, Liquid - methods</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General pharmacology</subject><subject>Humans</subject><subject>Immunoglobulin</subject><subject>Immunoglobulin G</subject><subject>Immunoglobulin G - isolation & purification</subject><subject>Immunoglobulins</subject><subject>Immunoglobulins - isolation & purification</subject><subject>Immunosorbent Techniques</subject><subject>Life Sciences</subject><subject>Mass spectrometry</subject><subject>Medical sciences</subject><subject>Pharmacology. Drug treatments</subject><subject>Serum</subject><subject>Sulfhydryl Compounds</subject><subject>Thiophilic adsorption</subject><issn>1570-0232</issn><issn>0378-4347</issn><issn>1873-376X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEQhoMo1q-foPai4GHXycdmd09Sil9Q8KLgLWSTWZqybWqyLfjvTemiRw9hQnjmncxDyCWFnAKV94t8YebBL5ucAcgcqhxoeUBOaFXyjJfy8zDdixIyYJyNyGmMC0gElPyYjKisRV3V7IRcv8-dX89d58xY2-jDund-NQ64ddH1aM_JUau7iBdDPSMfT4_v05ds9vb8Op3MMiMK2We64czasi6wAdoykMgLTmsrNLZYtsYKLipLDS1qbrBtbFNIWYCp0mm0Rn5G7va5c92pdXBLHb6V1069TGZq9wY8bSOAbWlib_fsOvivDcZeLV002HV6hX4TlawEEwzqBBZ70AQfY8D2N5mC2llUCzVYVDuLCiqVHKW-q2HAplmi_esatCXgZgB0NLprg14ZF_-4SsiSil3Qw57DpG7rMKhoHK4MWhfQ9Mp6989XfgCTxJHe</recordid><startdate>20070115</startdate><enddate>20070115</enddate><creator>Hardouin, Julie</creator><creator>Duchateau, Magalie</creator><creator>Canelle, Ludovic</creator><creator>Vlieghe, Céline</creator><creator>Joubert-Caron, Raymonde</creator><creator>Caron, Michel</creator><general>Elsevier B.V</general><general>Elsevier Science</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-4588-9811</orcidid><orcidid>https://orcid.org/0000-0001-5475-3065</orcidid></search><sort><creationdate>20070115</creationdate><title>Thiophilic adsorption revisited</title><author>Hardouin, Julie ; Duchateau, Magalie ; Canelle, Ludovic ; Vlieghe, Céline ; Joubert-Caron, Raymonde ; Caron, Michel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-ab32dd795eb01f206e35319d4aefe7fcd4348d1c1593cefbdb56650c850cbaae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adsorption</topic><topic>Analysis</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biochemistry, Molecular Biology</topic><topic>Biological and medical sciences</topic><topic>Chromatography, Liquid</topic><topic>Chromatography, Liquid - methods</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General pharmacology</topic><topic>Humans</topic><topic>Immunoglobulin</topic><topic>Immunoglobulin G</topic><topic>Immunoglobulin G - isolation & purification</topic><topic>Immunoglobulins</topic><topic>Immunoglobulins - isolation & purification</topic><topic>Immunosorbent Techniques</topic><topic>Life Sciences</topic><topic>Mass spectrometry</topic><topic>Medical sciences</topic><topic>Pharmacology. Drug treatments</topic><topic>Serum</topic><topic>Sulfhydryl Compounds</topic><topic>Thiophilic adsorption</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hardouin, Julie</creatorcontrib><creatorcontrib>Duchateau, Magalie</creatorcontrib><creatorcontrib>Canelle, Ludovic</creatorcontrib><creatorcontrib>Vlieghe, Céline</creatorcontrib><creatorcontrib>Joubert-Caron, Raymonde</creatorcontrib><creatorcontrib>Caron, Michel</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Journal of chromatography. B</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hardouin, Julie</au><au>Duchateau, Magalie</au><au>Canelle, Ludovic</au><au>Vlieghe, Céline</au><au>Joubert-Caron, Raymonde</au><au>Caron, Michel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thiophilic adsorption revisited</atitle><jtitle>Journal of chromatography. B</jtitle><addtitle>J Chromatogr B Analyt Technol Biomed Life Sci</addtitle><date>2007-01-15</date><risdate>2007</risdate><volume>845</volume><issue>2</issue><spage>226</spage><epage>231</epage><pages>226-231</pages><issn>1570-0232</issn><issn>0378-4347</issn><eissn>1873-376X</eissn><abstract>Specific and efficient selection of serum immunoglobulins, but not other proteins, on T-gel remains difficult. T-gel capacity was determined for different activation conditions and serum loadings. Mass spectrometry analysis was used to identify the proteins found in the flow-through and in the eluted fractions. Alpha-2-macroglobulin and albumin were the major contaminants of the eluates. The influence of the competition between immunoglobulins and the other serum proteins on the adsorption was also studied. Using a serum depleted in immunoglobulins (flow-through of a first chromatography on T-gel), many serum proteins were retained on the T-gel, including albumin. We conclude that T-gel selectivity is less than absolute and may reflect for a large part the experimental conditions of the adsorption.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>16949892</pmid><doi>10.1016/j.jchromb.2006.08.017</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0003-4588-9811</orcidid><orcidid>https://orcid.org/0000-0001-5475-3065</orcidid></addata></record> |
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subjects | Adsorption Analysis Analytical, structural and metabolic biochemistry Biochemistry, Molecular Biology Biological and medical sciences Chromatography, Liquid Chromatography, Liquid - methods Fundamental and applied biological sciences. Psychology General pharmacology Humans Immunoglobulin Immunoglobulin G Immunoglobulin G - isolation & purification Immunoglobulins Immunoglobulins - isolation & purification Immunosorbent Techniques Life Sciences Mass spectrometry Medical sciences Pharmacology. Drug treatments Serum Sulfhydryl Compounds Thiophilic adsorption |
title | Thiophilic adsorption revisited |
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