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Comparison of Different Electrophoretic Separations of Hen Egg White Proteins
The hen egg white protein composition has not yet been fully defined. To improve the knowledge of this biological fluid, the most usual and recently developed electrophoretic methods have been used: SDS−PAGE, native−PAGE, isoelectric focusing (IEF), and 2-dimensional electrophoresis (2DE). Seven of...
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Published in: | Journal of agricultural and food chemistry 2001-10, Vol.49 (10), p.4553-4561 |
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container_title | Journal of agricultural and food chemistry |
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creator | Desert, C Guérin-Dubiard, C Nau, F Jan, G Val, F Mallard, J |
description | The hen egg white protein composition has not yet been fully defined. To improve the knowledge of this biological fluid, the most usual and recently developed electrophoretic methods have been used: SDS−PAGE, native−PAGE, isoelectric focusing (IEF), and 2-dimensional electrophoresis (2DE). Seven of the major known proteins were thus identified in at least one electrophoretic system. Isoforms of ovotransferrin, ovalbumin, and ovomucoid were visualized when pI was used for the separation. Two-dimensional electrophoresis allowed separation of a very large number of spots. In each of the four systems, some components were revealed but not identified, and unknown spots were particularly numerous with 2DE. With this technique, many spots corresponding to small acidic proteins were highlighted, among which was the Ch21 protein, whose presence in hen egg white was thus confirmed. This study thus constitutes, to our knowledge, the first proteomic investigation of hen egg white. Keywords: Hen egg white; protein; SDS−PAGE; native−PAGE; IEF; two-dimensional gel electrophoresis; immunodetection; proteomic |
doi_str_mv | 10.1021/jf001423n |
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To improve the knowledge of this biological fluid, the most usual and recently developed electrophoretic methods have been used: SDS−PAGE, native−PAGE, isoelectric focusing (IEF), and 2-dimensional electrophoresis (2DE). Seven of the major known proteins were thus identified in at least one electrophoretic system. Isoforms of ovotransferrin, ovalbumin, and ovomucoid were visualized when pI was used for the separation. Two-dimensional electrophoresis allowed separation of a very large number of spots. In each of the four systems, some components were revealed but not identified, and unknown spots were particularly numerous with 2DE. With this technique, many spots corresponding to small acidic proteins were highlighted, among which was the Ch21 protein, whose presence in hen egg white was thus confirmed. This study thus constitutes, to our knowledge, the first proteomic investigation of hen egg white. Keywords: Hen egg white; protein; SDS−PAGE; native−PAGE; IEF; two-dimensional gel electrophoresis; immunodetection; proteomic</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf001423n</identifier><identifier>PMID: 11599987</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Animals ; Biological and medical sciences ; Blotting, Western ; Chickens ; Conalbumin - isolation & purification ; Egg and egg product industries ; Egg Proteins - isolation & purification ; Electrophoresis - methods ; Electrophoresis, Polyacrylamide Gel - methods ; Food engineering ; Food industries ; Fundamental and applied biological sciences. Psychology ; General aspects ; Isoelectric Focusing - methods ; Isoelectric Point ; Life Sciences ; Methods of analysis, processing and quality control, regulation, standards ; Ovalbumin - isolation & purification ; Ovomucin - isolation & purification</subject><ispartof>Journal of agricultural and food chemistry, 2001-10, Vol.49 (10), p.4553-4561</ispartof><rights>Copyright © 2001 American Chemical Society</rights><rights>2002 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a479t-5464808fc3d44eea28069250267a256e841ea931adab5a82dd42e6d816bd66f83</citedby><cites>FETCH-LOGICAL-a479t-5464808fc3d44eea28069250267a256e841ea931adab5a82dd42e6d816bd66f83</cites><orcidid>0000-0001-8694-3381 ; 0000-0002-0167-8759 ; 0000-0003-3824-6017 ; 0000-0001-7914-6034</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14094209$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11599987$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02673125$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Desert, C</creatorcontrib><creatorcontrib>Guérin-Dubiard, C</creatorcontrib><creatorcontrib>Nau, F</creatorcontrib><creatorcontrib>Jan, G</creatorcontrib><creatorcontrib>Val, F</creatorcontrib><creatorcontrib>Mallard, J</creatorcontrib><title>Comparison of Different Electrophoretic Separations of Hen Egg White Proteins</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>The hen egg white protein composition has not yet been fully defined. To improve the knowledge of this biological fluid, the most usual and recently developed electrophoretic methods have been used: SDS−PAGE, native−PAGE, isoelectric focusing (IEF), and 2-dimensional electrophoresis (2DE). Seven of the major known proteins were thus identified in at least one electrophoretic system. Isoforms of ovotransferrin, ovalbumin, and ovomucoid were visualized when pI was used for the separation. Two-dimensional electrophoresis allowed separation of a very large number of spots. In each of the four systems, some components were revealed but not identified, and unknown spots were particularly numerous with 2DE. With this technique, many spots corresponding to small acidic proteins were highlighted, among which was the Ch21 protein, whose presence in hen egg white was thus confirmed. This study thus constitutes, to our knowledge, the first proteomic investigation of hen egg white. Keywords: Hen egg white; protein; SDS−PAGE; native−PAGE; IEF; two-dimensional gel electrophoresis; immunodetection; proteomic</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Chickens</subject><subject>Conalbumin - isolation & purification</subject><subject>Egg and egg product industries</subject><subject>Egg Proteins - isolation & purification</subject><subject>Electrophoresis - methods</subject><subject>Electrophoresis, Polyacrylamide Gel - methods</subject><subject>Food engineering</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>Isoelectric Focusing - methods</subject><subject>Isoelectric Point</subject><subject>Life Sciences</subject><subject>Methods of analysis, processing and quality control, regulation, standards</subject><subject>Ovalbumin - isolation & purification</subject><subject>Ovomucin - isolation & purification</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><recordid>eNpt0E1vEzEQBmALgWgoHPgDaC8gcViwvbbXPlYhEKRUVGr5uFmT3XHjsLGD7aD237NRouTCaSTPo1eel5DXjH5glLOPa0cpE7wJT8iESU5ryZh-SiZ0XNZaKnZBXuS8ppRq2dLn5IIxaYzR7YRcT-NmC8nnGKroqk_eOUwYSjUbsCspblcxYfFddYsjg-JjyHs4x1DN7u-rnytfsLpJsaAP-SV55mDI-Oo4L8n3z7O76bxefPvydXq1qEG0ptRSKKGpdl3TC4EIXFNluKRctcClQi0YgmkY9LCUoHnfC46q10wte6Wcbi7J-0PuCga7TX4D6dFG8HZ-tbD7t31Uw7j8y0b77mC3Kf7ZYS5243OHwwAB4y7blnNKVcvOoV2KOSd0p2RG7b5ne-p5tG-OobvlBvuzPBY7grdHALmDwSUInc9nJ6gRnJrR1Qfnc8GH0x7Sbzte0Ep7d3NrfzDZ6l-NsdfnXOiyXcddCmPP__ngPw-8ngI</recordid><startdate>20011001</startdate><enddate>20011001</enddate><creator>Desert, C</creator><creator>Guérin-Dubiard, C</creator><creator>Nau, F</creator><creator>Jan, G</creator><creator>Val, F</creator><creator>Mallard, J</creator><general>American Chemical Society</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><scope>1XC</scope><orcidid>https://orcid.org/0000-0001-8694-3381</orcidid><orcidid>https://orcid.org/0000-0002-0167-8759</orcidid><orcidid>https://orcid.org/0000-0003-3824-6017</orcidid><orcidid>https://orcid.org/0000-0001-7914-6034</orcidid></search><sort><creationdate>20011001</creationdate><title>Comparison of Different Electrophoretic Separations of Hen Egg White Proteins</title><author>Desert, C ; Guérin-Dubiard, C ; Nau, F ; Jan, G ; Val, F ; Mallard, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a479t-5464808fc3d44eea28069250267a256e841ea931adab5a82dd42e6d816bd66f83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Chickens</topic><topic>Conalbumin - isolation & purification</topic><topic>Egg and egg product industries</topic><topic>Egg Proteins - isolation & purification</topic><topic>Electrophoresis - methods</topic><topic>Electrophoresis, Polyacrylamide Gel - methods</topic><topic>Food engineering</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects</topic><topic>Isoelectric Focusing - methods</topic><topic>Isoelectric Point</topic><topic>Life Sciences</topic><topic>Methods of analysis, processing and quality control, regulation, standards</topic><topic>Ovalbumin - isolation & purification</topic><topic>Ovomucin - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Desert, C</creatorcontrib><creatorcontrib>Guérin-Dubiard, C</creatorcontrib><creatorcontrib>Nau, F</creatorcontrib><creatorcontrib>Jan, G</creatorcontrib><creatorcontrib>Val, F</creatorcontrib><creatorcontrib>Mallard, J</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><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Desert, C</au><au>Guérin-Dubiard, C</au><au>Nau, F</au><au>Jan, G</au><au>Val, F</au><au>Mallard, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparison of Different Electrophoretic Separations of Hen Egg White Proteins</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2001-10-01</date><risdate>2001</risdate><volume>49</volume><issue>10</issue><spage>4553</spage><epage>4561</epage><pages>4553-4561</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>The hen egg white protein composition has not yet been fully defined. To improve the knowledge of this biological fluid, the most usual and recently developed electrophoretic methods have been used: SDS−PAGE, native−PAGE, isoelectric focusing (IEF), and 2-dimensional electrophoresis (2DE). Seven of the major known proteins were thus identified in at least one electrophoretic system. Isoforms of ovotransferrin, ovalbumin, and ovomucoid were visualized when pI was used for the separation. Two-dimensional electrophoresis allowed separation of a very large number of spots. In each of the four systems, some components were revealed but not identified, and unknown spots were particularly numerous with 2DE. With this technique, many spots corresponding to small acidic proteins were highlighted, among which was the Ch21 protein, whose presence in hen egg white was thus confirmed. This study thus constitutes, to our knowledge, the first proteomic investigation of hen egg white. Keywords: Hen egg white; protein; SDS−PAGE; native−PAGE; IEF; two-dimensional gel electrophoresis; immunodetection; proteomic</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>11599987</pmid><doi>10.1021/jf001423n</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0001-8694-3381</orcidid><orcidid>https://orcid.org/0000-0002-0167-8759</orcidid><orcidid>https://orcid.org/0000-0003-3824-6017</orcidid><orcidid>https://orcid.org/0000-0001-7914-6034</orcidid></addata></record> |
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subjects | Animals Biological and medical sciences Blotting, Western Chickens Conalbumin - isolation & purification Egg and egg product industries Egg Proteins - isolation & purification Electrophoresis - methods Electrophoresis, Polyacrylamide Gel - methods Food engineering Food industries Fundamental and applied biological sciences. Psychology General aspects Isoelectric Focusing - methods Isoelectric Point Life Sciences Methods of analysis, processing and quality control, regulation, standards Ovalbumin - isolation & purification Ovomucin - isolation & purification |
title | Comparison of Different Electrophoretic Separations of Hen Egg White Proteins |
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