Induction, purification and partial characterization of vitellogenin in an Indian major carp Catla catla (Ham.)
Identifieur interne : 001737 ( Istex/Corpus ); précédent : 001736; suivant : 001738Induction, purification and partial characterization of vitellogenin in an Indian major carp Catla catla (Ham.)
Auteurs : Bipulendu Jena ; Jyotirmaya Mohanty ; Radha C. Das ; Sushil K. Garnayak ; Samiran NandiSource :
- Aquaculture Research [ 1355-557X ] ; 2013-11.
Abstract
Vitellogenin was purified from the serum of 17‐β estradiol (E2)‐induced juvenile Catla catla using a simple two‐step purification procedure i.e. selective chemical precipitation followed by gel filtration chromatography. Purified protein migrated as single band in a native gradient PAGE which indicated the purity of the sample. The molecular weight of the native catla vitellogenin (~440 kDa) was determined using gel filtration chromatography. In SDS‐PAGE under reducing conditions catla vitellogenin dissociated into three major sub units at 115 kDa, 102 kDa and 73 kDa along with a few faint bands. Confirmation of purified protein as catla vitellogenin was supported by multiple physiological evidences, e.g. absence in male as well as juvenile sera and presence in matured female fish, ability to be synthesized upon estradiol injection in immature fish and certain unique biochemical properties like high molecular weight, phospholipoglycoprotein nature of the molecule. Western blot analysis showed that polyclonal antibody raised against purified protein detected vitellogenin in the sera of catla and in a few species selected from Cyprinidae family. These antisera were used to detect vitellogenin in liver tissue of hormone‐induced catla using immunohistochemistry and its applicability in other immunoassays is discussed.
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DOI: 10.1111/j.1365-2109.2012.03195.x
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E‐mail:</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: bjena@mdanderson.org</mods:affiliation></affiliation></author><author><name sortKey="Mohanty, Jyotirmaya" sort="Mohanty, Jyotirmaya" uniqKey="Mohanty J" first="Jyotirmaya" last="Mohanty">Jyotirmaya Mohanty</name><affiliation><mods:affiliation>Central Institute of Freshwater Aquaculture (CIFA), Bhubaneswar, India</mods:affiliation></affiliation></author><author><name sortKey="Das, Radha C" sort="Das, Radha C" uniqKey="Das R" first="Radha C" last="Das">Radha C. Das</name><affiliation><mods:affiliation>Central Institute of Fisheries Education (CIFE), Mumbai, India</mods:affiliation></affiliation></author><author><name sortKey="Garnayak, Sushil K" sort="Garnayak, Sushil K" uniqKey="Garnayak S" first="Sushil K" last="Garnayak">Sushil K. Garnayak</name><affiliation><mods:affiliation>Central Institute of Freshwater Aquaculture (CIFA), Bhubaneswar, India</mods:affiliation></affiliation></author><author><name sortKey="Nandi, Samiran" sort="Nandi, Samiran" uniqKey="Nandi S" first="Samiran" last="Nandi">Samiran Nandi</name><affiliation><mods:affiliation>Central Institute of Freshwater Aquaculture (CIFA), Bhubaneswar, India</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Aquaculture Research</title><title level="j" type="abbrev">Aquac Res</title><idno type="ISSN">1355-557X</idno><idno type="eISSN">1365-2109</idno><imprint><publisher>Blackwell Publishing Ltd</publisher><date type="published" when="2013-11">2013-11</date><biblScope unit="volume">44</biblScope><biblScope unit="issue">12</biblScope><biblScope unit="page" from="1901">1901</biblScope><biblScope unit="page" to="1911">1911</biblScope></imprint><idno type="ISSN">1355-557X</idno></series><idno type="istex">69C0E1F6A6EA2E19D28ED615CC8A2341A92495A7</idno><idno type="DOI">10.1111/j.1365-2109.2012.03195.x</idno><idno type="ArticleID">ARE3195</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1355-557X</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract">Vitellogenin was purified from the serum of 17‐β estradiol (E2)‐induced juvenile Catla catla using a simple two‐step purification procedure i.e. selective chemical precipitation followed by gel filtration chromatography. Purified protein migrated as single band in a native gradient PAGE which indicated the purity of the sample. The molecular weight of the native catla vitellogenin (~440 kDa) was determined using gel filtration chromatography. In SDS‐PAGE under reducing conditions catla vitellogenin dissociated into three major sub units at 115 kDa, 102 kDa and 73 kDa along with a few faint bands. Confirmation of purified protein as catla vitellogenin was supported by multiple physiological evidences, e.g. absence in male as well as juvenile sera and presence in matured female fish, ability to be synthesized upon estradiol injection in immature fish and certain unique biochemical properties like high molecular weight, phospholipoglycoprotein nature of the molecule. Western blot analysis showed that polyclonal antibody raised against purified protein detected vitellogenin in the sera of catla and in a few species selected from Cyprinidae family. 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Purified protein migrated as single band in a native gradient PAGE which indicated the purity of the sample. The molecular weight of the native catla vitellogenin (~440 kDa) was determined using gel filtration chromatography. In SDS‐PAGE under reducing conditions catla vitellogenin dissociated into three major sub units at 115 kDa, 102 kDa and 73 kDa along with a few faint bands. Confirmation of purified protein as catla vitellogenin was supported by multiple physiological evidences, e.g. absence in male as well as juvenile sera and presence in matured female fish, ability to be synthesized upon estradiol injection in immature fish and certain unique biochemical properties like high molecular weight, phospholipoglycoprotein nature of the molecule. Western blot analysis showed that polyclonal antibody raised against purified protein detected vitellogenin in the sera of catla and in a few species selected from Cyprinidae family. 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Purified protein migrated as single band in a native gradient PAGE which indicated the purity of the sample. The molecular weight of the native catla vitellogenin (~440 kDa) was determined using gel filtration chromatography. In SDS‐PAGE under reducing conditions catla vitellogenin dissociated into three major sub units at 115 kDa, 102 kDa and 73 kDa along with a few faint bands. Confirmation of purified protein as catla vitellogenin was supported by multiple physiological evidences, e.g. absence in male as well as juvenile sera and presence in matured female fish, ability to be synthesized upon estradiol injection in immature fish and certain unique biochemical properties like high molecular weight, phospholipoglycoprotein nature of the molecule. Western blot analysis showed that polyclonal antibody raised against purified protein detected vitellogenin in the sera of catla and in a few species selected from Cyprinidae family. These antisera were used to detect vitellogenin in liver tissue of hormone‐induced catla using immunohistochemistry and its applicability in other immunoassays is discussed.</p></abstract><textClass><keywords scheme="keyword"><list><head>keywords</head><item><term>Catla catla</term></item><item><term>vitellogenin</term></item><item><term>purification</term></item><item><term>characterization</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>article-category</head><item><term>Original Article</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2012-05-09">Created</change><change when="2013-11">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/69C0E1F6A6EA2E19D28ED615CC8A2341A92495A7/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component type="serialArticle" version="2.0" xml:id="are3195" xml:lang="en"><header><publicationMeta level="product"><doi origin="wiley" registered="yes">10.1111/(ISSN)1365-2109</doi><issn type="print">1355-557X</issn><issn type="electronic">1365-2109</issn><idGroup><id type="product" value="ARE"></id></idGroup><titleGroup><title sort="AQUACULTURE RESEARCH" type="main">Aquaculture Research</title><title type="short">Aquac Res</title></titleGroup></publicationMeta><publicationMeta level="part" position="120"><doi origin="wiley">10.1111/are.2013.44.issue-12</doi><copyright ownership="publisher">Copyright © 2013 John Wiley & Sons Ltd</copyright><numberingGroup><numbering type="journalVolume" number="44">44</numbering><numbering type="journalIssue">12</numbering></numberingGroup><coverDate startDate="2013-11">November 2013</coverDate></publicationMeta><publicationMeta level="unit" position="90" status="forIssue" type="article"><doi>10.1111/j.1365-2109.2012.03195.x</doi><idGroup><id type="unit" value="ARE3195"></id></idGroup><countGroup><count number="11" type="pageTotal"></count></countGroup><titleGroup><title type="articleCategory">Original Article</title><title type="tocHeading1">Original Articles</title></titleGroup><copyright ownership="publisher">© 2012 John Wiley & Sons Ltd</copyright><eventGroup><event agent="SPS" date="2012-05-09" type="xmlCreated"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.2.6 mode:FullText" date="2013-11-07"></event><event type="publishedOnlineEarlyUnpaginated" date="2012-07-05"></event><event type="firstOnline" date="2012-07-05"></event><event type="publishedOnlineFinalForm" date="2013-11-07"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.6.4 mode:FullText" date="2015-10-02"></event></eventGroup><numberingGroup><numbering type="pageFirst">1901</numbering><numbering type="pageLast">1911</numbering></numberingGroup><correspondenceTo><lineatedText><line><b>Correspondence:</b></line><line>B Jena, 7455 Fannin Street, SCR1 2014, Houston Texas‐77054 USA. E‐mail: <email>bjena@mdanderson.org</email></line></lineatedText></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:ARE.ARE3195.pdf"></link></linkGroup></publicationMeta><contentMeta><titleGroup><title type="main">Induction, purification and partial characterization of vitellogenin in an <fc>I</fc>ndian major carp <i><fc>C</fc>atla catla</i> (<fc>H</fc>am.)</title><title type="shortAuthors"><i>B Jena</i> et al.</title></titleGroup><creators><creator affiliationRef="#are3195-aff-0001" corresponding="yes" creatorRole="author" xml:id="are3195-cr-0001"><personName><givenNames>Bipulendu</givenNames> <familyName>Jena</familyName></personName></creator><creator affiliationRef="#are3195-aff-0001" creatorRole="author" xml:id="are3195-cr-0002"><personName><givenNames>Jyotirmaya</givenNames> <familyName>Mohanty</familyName></personName></creator><creator affiliationRef="#are3195-aff-0002" creatorRole="author" xml:id="are3195-cr-0003"><personName><givenNames>Radha C</givenNames> <familyName>Das</familyName></personName></creator><creator affiliationRef="#are3195-aff-0001" creatorRole="author" xml:id="are3195-cr-0004"><personName><givenNames>Sushil K</givenNames> <familyName>Garnayak</familyName></personName></creator><creator affiliationRef="#are3195-aff-0001" creatorRole="author" xml:id="are3195-cr-0005"><personName><givenNames>Samiran</givenNames> <familyName>Nandi</familyName></personName></creator></creators><affiliationGroup><affiliation countryCode="IN" type="organization" xml:id="are3195-aff-0001"><orgName>Central Institute of Freshwater Aquaculture (CIFA)</orgName> <address><city>Bhubaneswar</city> <country>India</country></address></affiliation><affiliation countryCode="IN" type="organization" xml:id="are3195-aff-0002"><orgName>Central Institute of Fisheries Education (CIFE)</orgName> <address><city>Mumbai</city> <country>India</country></address></affiliation></affiliationGroup><keywordGroup type="author"><keyword xml:id="are3195-kwd-0001"><i><fc>C</fc>atla catla</i></keyword><keyword xml:id="are3195-kwd-0002">vitellogenin</keyword><keyword xml:id="are3195-kwd-0003">purification</keyword><keyword xml:id="are3195-kwd-0004">characterization</keyword></keywordGroup><abstractGroup><abstract type="main" xml:id="are3195-abs-0001"><title type="main">Abstract</title><p>Vitellogenin was purified from the serum of 17‐β estradiol (E<sub>2</sub>)‐induced juvenile <i><fc>C</fc>atla catla</i> using a simple two‐step purification procedure i.e. selective chemical precipitation followed by gel filtration chromatography. Purified protein migrated as single band in a native gradient <fc>PAGE</fc> which indicated the purity of the sample. The molecular weight of the native catla vitellogenin (~440 kDa) was determined using gel filtration chromatography. In <fc>SDS</fc>‐<fc>PAGE</fc> under reducing conditions catla vitellogenin dissociated into three major sub units at 115 kDa, 102 kDa and 73 kDa along with a few faint bands. Confirmation of purified protein as catla vitellogenin was supported by multiple physiological evidences, e.g. absence in male as well as juvenile sera and presence in matured female fish, ability to be synthesized upon estradiol injection in immature fish and certain unique biochemical properties like high molecular weight, phospholipoglycoprotein nature of the molecule. Western blot analysis showed that polyclonal antibody raised against purified protein detected vitellogenin in the sera of catla and in a few species selected from <fc>C</fc>yprinidae family. These antisera were used to detect vitellogenin in liver tissue of hormone‐induced catla using immunohistochemistry and its applicability in other immunoassays is discussed.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Induction, purification and partial characterization of vitellogenin in an Indian major carp Catla catla (Ham.)</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Induction, purification and partial characterization of vitellogenin in an Indian major carp Catla catla (Ham.)</title></titleInfo><name type="personal"><namePart type="given">Bipulendu</namePart><namePart type="family">Jena</namePart><affiliation>Central Institute of Freshwater Aquaculture (CIFA), Bhubaneswar, India</affiliation><affiliation>B Jena, 7455 Fannin Street, SCR1 2014, Houston Texas‐77054 USA. E‐mail:</affiliation><affiliation>E-mail: bjena@mdanderson.org</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jyotirmaya</namePart><namePart type="family">Mohanty</namePart><affiliation>Central Institute of Freshwater Aquaculture (CIFA), Bhubaneswar, India</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Radha C</namePart><namePart type="family">Das</namePart><affiliation>Central Institute of Fisheries Education (CIFE), Mumbai, India</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Sushil K</namePart><namePart type="family">Garnayak</namePart><affiliation>Central Institute of Freshwater Aquaculture (CIFA), Bhubaneswar, India</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Samiran</namePart><namePart type="family">Nandi</namePart><affiliation>Central Institute of Freshwater Aquaculture (CIFA), Bhubaneswar, India</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><dateIssued encoding="w3cdtf">2013-11</dateIssued><dateCreated encoding="w3cdtf">2012-05-09</dateCreated><copyrightDate encoding="w3cdtf">2013</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract>Vitellogenin was purified from the serum of 17‐β estradiol (E2)‐induced juvenile Catla catla using a simple two‐step purification procedure i.e. selective chemical precipitation followed by gel filtration chromatography. Purified protein migrated as single band in a native gradient PAGE which indicated the purity of the sample. The molecular weight of the native catla vitellogenin (~440 kDa) was determined using gel filtration chromatography. In SDS‐PAGE under reducing conditions catla vitellogenin dissociated into three major sub units at 115 kDa, 102 kDa and 73 kDa along with a few faint bands. Confirmation of purified protein as catla vitellogenin was supported by multiple physiological evidences, e.g. absence in male as well as juvenile sera and presence in matured female fish, ability to be synthesized upon estradiol injection in immature fish and certain unique biochemical properties like high molecular weight, phospholipoglycoprotein nature of the molecule. Western blot analysis showed that polyclonal antibody raised against purified protein detected vitellogenin in the sera of catla and in a few species selected from Cyprinidae family. These antisera were used to detect vitellogenin in liver tissue of hormone‐induced catla using immunohistochemistry and its applicability in other immunoassays is discussed.</abstract><subject><genre>keywords</genre><topic>Catla catla</topic><topic>vitellogenin</topic><topic>purification</topic><topic>characterization</topic></subject><relatedItem type="host"><titleInfo><title>Aquaculture Research</title></titleInfo><titleInfo type="abbreviated"><title>Aquac Res</title></titleInfo><genre type="journal">journal</genre><subject><genre>article-category</genre><topic>Original Article</topic></subject><identifier type="ISSN">1355-557X</identifier><identifier type="eISSN">1365-2109</identifier><identifier type="DOI">10.1111/(ISSN)1365-2109</identifier><identifier type="PublisherID">ARE</identifier><part><date>2013</date><detail type="volume"><caption>vol.</caption><number>44</number></detail><detail type="issue"><caption>no.</caption><number>12</number></detail><extent unit="pages"><start>1901</start><end>1911</end><total>11</total></extent></part></relatedItem><identifier type="istex">69C0E1F6A6EA2E19D28ED615CC8A2341A92495A7</identifier><identifier type="DOI">10.1111/j.1365-2109.2012.03195.x</identifier><identifier type="ArticleID">ARE3195</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2013 John Wiley & Sons Ltd© 2012 John Wiley & Sons Ltd</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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