Protein Isolation by Solution-Controlled Gel Sorption
Illustrated are the principles for isolating proteins from solution by sorption into a polymer gel phase, driven by the addition of a water‐soluble polymer to the protein solution. The separation is shown to be analogous to conventional two‐phase aqueous extraction. However, the use of a gel phase r...
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Veröffentlicht in: | Biotechnology progress 1991-07, Vol.7 (4), p.355-358 |
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creator | Gehrke, Stevin H. Robeson, Julie Johnson, James Fred Vaid, Nitin |
description | Illustrated are the principles for isolating proteins from solution by sorption into a polymer gel phase, driven by the addition of a water‐soluble polymer to the protein solution. The separation is shown to be analogous to conventional two‐phase aqueous extraction. However, the use of a gel phase rather than a solution for absorbing the protein makes separation of the protein from the polymer and the recycling of the gel phase much simpler. The model system used was linear poly(ethylene glycol) (PEG) and dextran gel. Increasing the molecular weight and concentration of the PEG favored sorption by the gel of ovalbumin, bovine serum albumin, cytochrome c, and hemoglobin. The proteins could be quantitatively recovered by immersing the gel in PEG‐free solution. |
doi_str_mv | 10.1021/bp00010a010 |
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The separation is shown to be analogous to conventional two‐phase aqueous extraction. However, the use of a gel phase rather than a solution for absorbing the protein makes separation of the protein from the polymer and the recycling of the gel phase much simpler. The model system used was linear poly(ethylene glycol) (PEG) and dextran gel. Increasing the molecular weight and concentration of the PEG favored sorption by the gel of ovalbumin, bovine serum albumin, cytochrome c, and hemoglobin. The proteins could be quantitatively recovered by immersing the gel in PEG‐free solution.</description><identifier>ISSN: 8756-7938</identifier><identifier>EISSN: 1520-6033</identifier><identifier>DOI: 10.1021/bp00010a010</identifier><identifier>PMID: 1370046</identifier><identifier>CODEN: BIPRET</identifier><language>eng</language><publisher>USA: American Chemical Society</publisher><subject>Biological and medical sciences ; Biotechnology ; Chemistry Techniques, Analytical - methods ; Chromatography - methods ; Cytochrome c Group - isolation & purification ; Dextrans ; Fundamental and applied biological sciences. Psychology ; Gels - chemistry ; Methods. Procedures. 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The separation is shown to be analogous to conventional two‐phase aqueous extraction. However, the use of a gel phase rather than a solution for absorbing the protein makes separation of the protein from the polymer and the recycling of the gel phase much simpler. The model system used was linear poly(ethylene glycol) (PEG) and dextran gel. Increasing the molecular weight and concentration of the PEG favored sorption by the gel of ovalbumin, bovine serum albumin, cytochrome c, and hemoglobin. The proteins could be quantitatively recovered by immersing the gel in PEG‐free solution.</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chemistry Techniques, Analytical - methods</subject><subject>Chromatography - methods</subject><subject>Cytochrome c Group - isolation & purification</subject><subject>Dextrans</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels - chemistry</subject><subject>Methods. Procedures. Technologies</subject><subject>Others</subject><subject>Polyethylene Glycols</subject><subject>Proteins - isolation & purification</subject><subject>Solutions</subject><subject>Various methods and equipments</subject><issn>8756-7938</issn><issn>1520-6033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1LAzEQxYMoWj9OnoVe9CKrk49Ndo9abBVEpVYULyHNJrCabmqyRfvfm7JFPXkICTO_92byEDrEcIaB4PPpHAAwqHQ2UA_nBDIOlG6iXiFynomSFjtoN8a3hBXAyTbaxlQAMN5D-UPwramb_k30TrW1b_rTZf_Ru8XqnQ180wbvnKn6I-NSPcxX9X20ZZWL5mB976Gn4dVkcJ3d3o9uBhe3mWaU48zkTE0tcMGBV1RbQ5i2oG2hlAYDNNdYaEUs5xYzUJW2JDGcVaqsFAND99BJ5zsP_mNhYitnddTGOdUYv4hSEEj_oGUCTztQBx9jMFbOQz1TYSkxyFVI8k9IiT5a2y6mM1P9sl0qqX-87quolbNBNbqOv1hZEIZLkTjRcZ-1M8v_RsrLycM4ZwTSvgzjpMw6ZR1b8_WjVOFdckFFLp_vRnI4HA9eyOWrZPQbbYOODQ</recordid><startdate>199107</startdate><enddate>199107</enddate><creator>Gehrke, Stevin H.</creator><creator>Robeson, Julie</creator><creator>Johnson, James Fred</creator><creator>Vaid, Nitin</creator><general>American Chemical Society</general><general>American Institute of Chemical Engineers</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>199107</creationdate><title>Protein Isolation by Solution-Controlled Gel Sorption</title><author>Gehrke, Stevin H. ; Robeson, Julie ; Johnson, James Fred ; Vaid, Nitin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4361-e54abf067606d3cfe24cf0cf8aac0e035c17ca2f66f140adcf2fe264da9da40e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Chemistry Techniques, Analytical - methods</topic><topic>Chromatography - methods</topic><topic>Cytochrome c Group - isolation & purification</topic><topic>Dextrans</topic><topic>Fundamental and applied biological sciences. 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Technologies</topic><topic>Others</topic><topic>Polyethylene Glycols</topic><topic>Proteins - isolation & purification</topic><topic>Solutions</topic><topic>Various methods and equipments</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gehrke, Stevin H.</creatorcontrib><creatorcontrib>Robeson, Julie</creatorcontrib><creatorcontrib>Johnson, James Fred</creatorcontrib><creatorcontrib>Vaid, Nitin</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>Biotechnology progress</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gehrke, Stevin H.</au><au>Robeson, Julie</au><au>Johnson, James Fred</au><au>Vaid, Nitin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein Isolation by Solution-Controlled Gel Sorption</atitle><jtitle>Biotechnology progress</jtitle><addtitle>Biotechnol Progress</addtitle><date>1991-07</date><risdate>1991</risdate><volume>7</volume><issue>4</issue><spage>355</spage><epage>358</epage><pages>355-358</pages><issn>8756-7938</issn><eissn>1520-6033</eissn><coden>BIPRET</coden><abstract>Illustrated are the principles for isolating proteins from solution by sorption into a polymer gel phase, driven by the addition of a water‐soluble polymer to the protein solution. The separation is shown to be analogous to conventional two‐phase aqueous extraction. However, the use of a gel phase rather than a solution for absorbing the protein makes separation of the protein from the polymer and the recycling of the gel phase much simpler. The model system used was linear poly(ethylene glycol) (PEG) and dextran gel. Increasing the molecular weight and concentration of the PEG favored sorption by the gel of ovalbumin, bovine serum albumin, cytochrome c, and hemoglobin. The proteins could be quantitatively recovered by immersing the gel in PEG‐free solution.</abstract><cop>USA</cop><pub>American Chemical Society</pub><pmid>1370046</pmid><doi>10.1021/bp00010a010</doi><tpages>4</tpages></addata></record> |
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subjects | Biological and medical sciences Biotechnology Chemistry Techniques, Analytical - methods Chromatography - methods Cytochrome c Group - isolation & purification Dextrans Fundamental and applied biological sciences. Psychology Gels - chemistry Methods. Procedures. Technologies Others Polyethylene Glycols Proteins - isolation & purification Solutions Various methods and equipments |
title | Protein Isolation by Solution-Controlled Gel Sorption |
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