Thiophilic Interaction Chromatography of Serum Albumins
An investigation of the binding of native and recombinant human serum albumin and bovine serum albumin on three thiophilic gels, PyS, 2S, and 3S was performed. In addition to these proteins, we studied serum albumins from several species such as goat, rabbit, guinea pig, rat, hamster, baboon, and pi...
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| Veröffentlicht in: | Journal of chromatographic science 2008-07, Vol.46 (6), p.574-576 |
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| container_title | Journal of chromatographic science |
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| creator | Bourhim, Mustapha Rajendran, Anita Ramos, Yanira Srikrishnan, Thamarapu Sulkowski, Eugene |
| description | An investigation of the binding of native and recombinant human serum albumin and bovine serum albumin on three thiophilic gels, PyS, 2S, and 3S was performed. In addition to these proteins, we studied serum albumins from several species such as goat, rabbit, guinea pig, rat, hamster, baboon, and pig. Our results reveal that recombinant human serum albumin (rHSA) binds completely to PyS whereas native human serum albumin and bovine serum albumin bind only partially to PyS. The binding affinities of rHSA, human serum albumin and bovine serum albumin to 2S and 3S gels are less than their binding to PyS. Serum albumins from goat, rabbit, guinea pig, rat, hamster, baboon, and pig bind much stronger to 3S gel than human and bovine serum albumins. The binding of pig and hamster serum albumins is stronger than that of rat, goat, baboon, and rabbit. |
| doi_str_mv | 10.1093/chromsci/46.6.574 |
| format | Article |
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In addition to these proteins, we studied serum albumins from several species such as goat, rabbit, guinea pig, rat, hamster, baboon, and pig. Our results reveal that recombinant human serum albumin (rHSA) binds completely to PyS whereas native human serum albumin and bovine serum albumin bind only partially to PyS. The binding affinities of rHSA, human serum albumin and bovine serum albumin to 2S and 3S gels are less than their binding to PyS. Serum albumins from goat, rabbit, guinea pig, rat, hamster, baboon, and pig bind much stronger to 3S gel than human and bovine serum albumins. The binding of pig and hamster serum albumins is stronger than that of rat, goat, baboon, and rabbit.</description><identifier>ISSN: 0021-9665</identifier><identifier>EISSN: 1945-239X</identifier><identifier>DOI: 10.1093/chromsci/46.6.574</identifier><identifier>PMID: 18647483</identifier><identifier>CODEN: JCHSBZ</identifier><language>eng</language><publisher>Niles, IL: Oxford University Press</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cattle ; Chromatography, High Pressure Liquid - methods ; Fundamental and applied biological sciences. 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In addition to these proteins, we studied serum albumins from several species such as goat, rabbit, guinea pig, rat, hamster, baboon, and pig. Our results reveal that recombinant human serum albumin (rHSA) binds completely to PyS whereas native human serum albumin and bovine serum albumin bind only partially to PyS. The binding affinities of rHSA, human serum albumin and bovine serum albumin to 2S and 3S gels are less than their binding to PyS. Serum albumins from goat, rabbit, guinea pig, rat, hamster, baboon, and pig bind much stronger to 3S gel than human and bovine serum albumins. The binding of pig and hamster serum albumins is stronger than that of rat, goat, baboon, and rabbit.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Chromatography, High Pressure Liquid - methods</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects, investigation methods</subject><subject>Humans</subject><subject>Proteins</subject><subject>Recombinant Proteins - chemistry</subject><subject>Serum Albumin - chemistry</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrophotometry, Ultraviolet</subject><issn>0021-9665</issn><issn>1945-239X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkF1LwzAYhYMobk5_gDfSG72yM99JL2X4BQNFJ8huQpqlLto2NWnB_Xs7NuetVy8HnnNeeAA4RXCMYEauzDL4Khp3RfmYj5mge2CIMspSTLK3fTCEEKM045wNwFGMH-uIJDsEAyQ5FVSSIRCzpfPN0pXOJA91a4M2rfN1MllP69a_B90sV4kvkhcbuiq5LvOucnU8BgeFLqM92d4ReL29mU3u0-nj3cPkepoaKmCbUpGzRZGjIkNWMmMp1owYmhc5wUhCYRaCCIyNkBkkAmJmFxIbg40VEuUSkRG42Ow2wX91NraqctHYstS19V1UPCNE0mwNog1ogo8x2EI1wVU6rBSCam1L_dpSlCuuelt952w73uWVXfw1tnp64HwL6Gh0WQRdGxd3HIZUIC5kz11uON81__qbbnAXW_u9K-jwqXjvg6n7t7mS82c5eZrO1JT8ADeXkq0</recordid><startdate>20080701</startdate><enddate>20080701</enddate><creator>Bourhim, Mustapha</creator><creator>Rajendran, Anita</creator><creator>Ramos, Yanira</creator><creator>Srikrishnan, Thamarapu</creator><creator>Sulkowski, Eugene</creator><general>Oxford University Press</general><general>Preston Publications</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>20080701</creationdate><title>Thiophilic Interaction Chromatography of Serum Albumins</title><author>Bourhim, Mustapha ; Rajendran, Anita ; Ramos, Yanira ; Srikrishnan, Thamarapu ; Sulkowski, Eugene</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c470t-47b5dfb1f91e85ce42a53c4bfb321807cd73722c789037025ed82cc2ce781b813</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Chromatography, High Pressure Liquid - methods</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects, investigation methods</topic><topic>Humans</topic><topic>Proteins</topic><topic>Recombinant Proteins - chemistry</topic><topic>Serum Albumin - chemistry</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectrophotometry, Ultraviolet</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bourhim, Mustapha</creatorcontrib><creatorcontrib>Rajendran, Anita</creatorcontrib><creatorcontrib>Ramos, Yanira</creatorcontrib><creatorcontrib>Srikrishnan, Thamarapu</creatorcontrib><creatorcontrib>Sulkowski, Eugene</creatorcontrib><collection>Istex</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>MEDLINE - Academic</collection><jtitle>Journal of chromatographic science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bourhim, Mustapha</au><au>Rajendran, Anita</au><au>Ramos, Yanira</au><au>Srikrishnan, Thamarapu</au><au>Sulkowski, Eugene</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thiophilic Interaction Chromatography of Serum Albumins</atitle><jtitle>Journal of chromatographic science</jtitle><stitle>Journal of Chromatographic Science</stitle><addtitle>Journal of Chromatographic Science</addtitle><date>2008-07-01</date><risdate>2008</risdate><volume>46</volume><issue>6</issue><spage>574</spage><epage>576</epage><pages>574-576</pages><issn>0021-9665</issn><eissn>1945-239X</eissn><coden>JCHSBZ</coden><abstract>An investigation of the binding of native and recombinant human serum albumin and bovine serum albumin on three thiophilic gels, PyS, 2S, and 3S was performed. In addition to these proteins, we studied serum albumins from several species such as goat, rabbit, guinea pig, rat, hamster, baboon, and pig. Our results reveal that recombinant human serum albumin (rHSA) binds completely to PyS whereas native human serum albumin and bovine serum albumin bind only partially to PyS. The binding affinities of rHSA, human serum albumin and bovine serum albumin to 2S and 3S gels are less than their binding to PyS. Serum albumins from goat, rabbit, guinea pig, rat, hamster, baboon, and pig bind much stronger to 3S gel than human and bovine serum albumins. The binding of pig and hamster serum albumins is stronger than that of rat, goat, baboon, and rabbit.</abstract><cop>Niles, IL</cop><pub>Oxford University Press</pub><pmid>18647483</pmid><doi>10.1093/chromsci/46.6.574</doi><tpages>3</tpages></addata></record> |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cattle Chromatography, High Pressure Liquid - methods Fundamental and applied biological sciences. Psychology General aspects, investigation methods Humans Proteins Recombinant Proteins - chemistry Serum Albumin - chemistry Spectrometry, Fluorescence Spectrophotometry, Ultraviolet |
| title | Thiophilic Interaction Chromatography of Serum Albumins |
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