Thiophilic adsorption - a new method for protein fractionation
Divinylsulphone-activated agarose to which mercaptoethanol is coupled showed very selective group adsorption of human serum proteins, in particular the immunoglobulins. The adsorption increases markedly in the presence of high concentrations of neutral water-structure forming salts and is distinct f...
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| Veröffentlicht in: | FEBS letters 1985-06, Vol.185 (2), p.306-310 |
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| creator | Porath, Jerker Maisano, Federico Belew, Makonnen |
| description | Divinylsulphone-activated agarose to which mercaptoethanol is coupled showed very selective group adsorption of human serum proteins, in particular the immunoglobulins. The adsorption increases markedly in the presence of high concentrations of neutral water-structure forming salts and is distinct from adsorptions based on hydrophobic interaction. A characteristic feature of this new type of adsorbent is the structure of the groups attached to the polymer, XXX, i.e., R-S-CH
2-CH
2-SO
2-CH
2-CH
2-O-XXX, where R is a small aliphatic residue. Our results indicate that the thioether sulphur and the adjacent sulphone group act cooperatively and are apparently necessary to maintain the distinct behaviour of such absorbents.
Divinylsulfone
Immunoglobulin
Affinity chromatography
Hydrophobic interaction (salting-out)
Serum fractionation |
| doi_str_mv | 10.1016/0014-5793(85)80928-5 |
| format | Article |
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2-CH
2-SO
2-CH
2-CH
2-O-XXX, where R is a small aliphatic residue. Our results indicate that the thioether sulphur and the adjacent sulphone group act cooperatively and are apparently necessary to maintain the distinct behaviour of such absorbents.
Divinylsulfone
Immunoglobulin
Affinity chromatography
Hydrophobic interaction (salting-out)
Serum fractionation</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(85)80928-5</identifier><identifier>PMID: 3996606</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Adsorption ; affinity chromatography ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Blood Proteins - analysis ; Chromatography, Affinity - methods ; Fundamental and applied biological sciences. Psychology ; Gels ; General aspects, investigation methods ; Humans ; immunoglobulins ; Immunoglobulins - analysis ; man ; Polymers ; Proteins ; Rats ; serum ; Sulfones</subject><ispartof>FEBS letters, 1985-06, Vol.185 (2), p.306-310</ispartof><rights>1985</rights><rights>FEBS Letters 185 (1985) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5925-847f772b07512f77cbef4637779725cd7eefa1ed820a4ead24c91ebd4953c40a3</citedby><cites>FETCH-LOGICAL-c5925-847f772b07512f77cbef4637779725cd7eefa1ed820a4ead24c91ebd4953c40a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(85)80928-5$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8546384$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3996606$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Porath, Jerker</creatorcontrib><creatorcontrib>Maisano, Federico</creatorcontrib><creatorcontrib>Belew, Makonnen</creatorcontrib><title>Thiophilic adsorption - a new method for protein fractionation</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Divinylsulphone-activated agarose to which mercaptoethanol is coupled showed very selective group adsorption of human serum proteins, in particular the immunoglobulins. The adsorption increases markedly in the presence of high concentrations of neutral water-structure forming salts and is distinct from adsorptions based on hydrophobic interaction. A characteristic feature of this new type of adsorbent is the structure of the groups attached to the polymer, XXX, i.e., R-S-CH
2-CH
2-SO
2-CH
2-CH
2-O-XXX, where R is a small aliphatic residue. Our results indicate that the thioether sulphur and the adjacent sulphone group act cooperatively and are apparently necessary to maintain the distinct behaviour of such absorbents.
Divinylsulfone
Immunoglobulin
Affinity chromatography
Hydrophobic interaction (salting-out)
Serum fractionation</description><subject>Adsorption</subject><subject>affinity chromatography</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blood Proteins - analysis</subject><subject>Chromatography, Affinity - methods</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>General aspects, investigation methods</subject><subject>Humans</subject><subject>immunoglobulins</subject><subject>Immunoglobulins - analysis</subject><subject>man</subject><subject>Polymers</subject><subject>Proteins</subject><subject>Rats</subject><subject>serum</subject><subject>Sulfones</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEtPGzEQgK2KCgLtPyjSHlAFh239XNuXSAWRthJSL_RsOfas4mqzDvYGxL-vTaIcgYsfM9-Mxx9CXwj-RjDpvmNMeCukZpdKXCmsqWrFBzQjSrKW8U4dodkBOUGnOf_D5a6IPkbHTOuuw90Mze9XIW5WYQiusT7HtJlCHJu2sc0IT80aplX0TR9Ts0lxgjA2fbKuMrYun9DH3g4ZPu_3M_R3cXt_86u9-_Pz982Pu9YJTUWruOylpEssBaHl5JbQ845JKbWkwnkJ0FsCXlFsOVhPudMElp5rwRzHlp2hr7u-ZYqHLeTJrEN2MAx2hLjNRnYEM9WRN0HCGSZUVpDvQJdizgl6s0lhbdOzIdhUv6bKM1WeUcK8-DWilJ3v-2-Xa_CHor3Qkr_Y5212diiyRhfyAVOifFvxgi122FMY4PldT5vF7TWtiRpX4iVa55nvGkGx_xggmewCjA58SOAm42N4_UP_AfzgqMQ</recordid><startdate>19850617</startdate><enddate>19850617</enddate><creator>Porath, Jerker</creator><creator>Maisano, Federico</creator><creator>Belew, Makonnen</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19850617</creationdate><title>Thiophilic adsorption - a new method for protein fractionation</title><author>Porath, Jerker ; Maisano, Federico ; Belew, Makonnen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5925-847f772b07512f77cbef4637779725cd7eefa1ed820a4ead24c91ebd4953c40a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Adsorption</topic><topic>affinity chromatography</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blood Proteins - analysis</topic><topic>Chromatography, Affinity - methods</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>General aspects, investigation methods</topic><topic>Humans</topic><topic>immunoglobulins</topic><topic>Immunoglobulins - analysis</topic><topic>man</topic><topic>Polymers</topic><topic>Proteins</topic><topic>Rats</topic><topic>serum</topic><topic>Sulfones</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Porath, Jerker</creatorcontrib><creatorcontrib>Maisano, Federico</creatorcontrib><creatorcontrib>Belew, Makonnen</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Porath, Jerker</au><au>Maisano, Federico</au><au>Belew, Makonnen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thiophilic adsorption - a new method for protein fractionation</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1985-06-17</date><risdate>1985</risdate><volume>185</volume><issue>2</issue><spage>306</spage><epage>310</epage><pages>306-310</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Divinylsulphone-activated agarose to which mercaptoethanol is coupled showed very selective group adsorption of human serum proteins, in particular the immunoglobulins. The adsorption increases markedly in the presence of high concentrations of neutral water-structure forming salts and is distinct from adsorptions based on hydrophobic interaction. A characteristic feature of this new type of adsorbent is the structure of the groups attached to the polymer, XXX, i.e., R-S-CH
2-CH
2-SO
2-CH
2-CH
2-O-XXX, where R is a small aliphatic residue. Our results indicate that the thioether sulphur and the adjacent sulphone group act cooperatively and are apparently necessary to maintain the distinct behaviour of such absorbents.
Divinylsulfone
Immunoglobulin
Affinity chromatography
Hydrophobic interaction (salting-out)
Serum fractionation</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>3996606</pmid><doi>10.1016/0014-5793(85)80928-5</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1985-06, Vol.185 (2), p.306-310 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; ScienceDirect Journals (5 years ago - present); Alma/SFX Local Collection |
| subjects | Adsorption affinity chromatography Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Blood Proteins - analysis Chromatography, Affinity - methods Fundamental and applied biological sciences. Psychology Gels General aspects, investigation methods Humans immunoglobulins Immunoglobulins - analysis man Polymers Proteins Rats serum Sulfones |
| title | Thiophilic adsorption - a new method for protein fractionation |
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