Identification of the Second Form of Acrosin in Turkey Spermatozoa
Identifieur interne : 001595 ( Istex/Corpus ); précédent : 001594; suivant : 001596Identification of the Second Form of Acrosin in Turkey Spermatozoa
Auteurs : M. Słowi Ska ; A. CiereszkoSource :
- Reproduction in Domestic Animals [ 0936-6768 ] ; 2012-10.
Abstract
Acrosin from turkey spermatozoa has been recently identified and characterized. In this study, we reported the identification of second form of acrosin (acrosin II) in turkey spermatozoa. Using the three‐step isolation procedure, we purified and characterized the acrosin II from a turkey spermatozoa extract. N‐terminal Edman sequencing allowed the identification of the 24 amino acids from the internal part of acrosin II: SLQEYVEPYRVLQEAKVQLIDLNL. Thanks to homology alignment, we concluded that acrosin II is an acrosin‐like protein similar to avian acrosin, including turkey acrosin. The molecular mass of acrosin II estimated by mass spectrometry was 30.869 kDa. During chromatofocusing, the acrosin II was eluted at pH range from 6.4 to 6.2. Acrosin II was found to be a glycoprotein. The glucosamine and galactosamine were present in carbohydrate structures of acrosin II. Acrosin II is characterized by similar physicochemical characteristics like previously identified bird acrosins, including acrosin from turkey spermatozoa. Similarities between turkey acrosins were also confirmed immunologically by western blot analysis. It can be suggested that two forms of serine proteinase similar to acrosin exist in turkey spermatozoa. These phenomena of both acrosins in spermatozoa agree with the concept of functional redundancy of proteolytic enzymes in the reproductive system. These redundancies may be important for efficient fertilization in turkey.
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DOI: 10.1111/j.1439-0531.2011.01981.x
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Ciereszko</name><affiliation><mods:affiliation>Department of Gamete and Embryo Biology, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences in Olsztyn, Tuwima, Olsztyn, Poland</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:AF8FC289B6270429602559B82FA3119BB0094557</idno><date when="2012" year="2012">2012</date><idno type="doi">10.1111/j.1439-0531.2011.01981.x</idno><idno type="url">https://api.istex.fr/document/AF8FC289B6270429602559B82FA3119BB0094557/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001595</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001595</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Identification of the Second Form of Acrosin in Turkey Spermatozoa</title><author><name sortKey="Slowi Ska, M" sort="Slowi Ska, M" uniqKey="Slowi Ska M" first="M" last="Słowi Ska">M. Słowi Ska</name><affiliation><mods:affiliation>Department of Gamete and Embryo Biology, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences in Olsztyn, Tuwima, Olsztyn, Poland</mods:affiliation></affiliation></author><author><name sortKey="Ciereszko, A" sort="Ciereszko, A" uniqKey="Ciereszko A" first="A" last="Ciereszko">A. Ciereszko</name><affiliation><mods:affiliation>Department of Gamete and Embryo Biology, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences in Olsztyn, Tuwima, Olsztyn, Poland</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Reproduction in Domestic Animals</title><idno type="ISSN">0936-6768</idno><idno type="eISSN">1439-0531</idno><imprint><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="2012-10">2012-10</date><biblScope unit="volume">47</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="849">849</biblScope><biblScope unit="page" to="855">855</biblScope></imprint><idno type="ISSN">0936-6768</idno></series><idno type="istex">AF8FC289B6270429602559B82FA3119BB0094557</idno><idno type="DOI">10.1111/j.1439-0531.2011.01981.x</idno><idno type="ArticleID">RDA1981</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0936-6768</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Acrosin from turkey spermatozoa has been recently identified and characterized. In this study, we reported the identification of second form of acrosin (acrosin II) in turkey spermatozoa. Using the three‐step isolation procedure, we purified and characterized the acrosin II from a turkey spermatozoa extract. N‐terminal Edman sequencing allowed the identification of the 24 amino acids from the internal part of acrosin II: SLQEYVEPYRVLQEAKVQLIDLNL. Thanks to homology alignment, we concluded that acrosin II is an acrosin‐like protein similar to avian acrosin, including turkey acrosin. The molecular mass of acrosin II estimated by mass spectrometry was 30.869 kDa. During chromatofocusing, the acrosin II was eluted at pH range from 6.4 to 6.2. Acrosin II was found to be a glycoprotein. The glucosamine and galactosamine were present in carbohydrate structures of acrosin II. Acrosin II is characterized by similar physicochemical characteristics like previously identified bird acrosins, including acrosin from turkey spermatozoa. Similarities between turkey acrosins were also confirmed immunologically by western blot analysis. It can be suggested that two forms of serine proteinase similar to acrosin exist in turkey spermatozoa. These phenomena of both acrosins in spermatozoa agree with the concept of functional redundancy of proteolytic enzymes in the reproductive system. 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Similarities between turkey acrosins were also confirmed immunologically by western blot analysis. It can be suggested that two forms of serine proteinase similar to acrosin exist in turkey spermatozoa. These phenomena of both acrosins in spermatozoa agree with the concept of functional redundancy of proteolytic enzymes in the reproductive system. 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Similarities between turkey acrosins were also confirmed immunologically by western blot analysis. It can be suggested that two forms of serine proteinase similar to acrosin exist in turkey spermatozoa. These phenomena of both acrosins in spermatozoa agree with the concept of functional redundancy of proteolytic enzymes in the reproductive system. 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E‐mail: <email>m.slowinska@pan.olsztyn.pl</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:RDA.RDA1981.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Submitted: 21 May 2011; Accepted: 15 Dec 2011</unparsedEditorialHistory><countGroup><count type="figureTotal" number="5"></count><count type="tableTotal" number="0"></count></countGroup><titleGroup><title type="main">Identification of the Second Form of Acrosin in Turkey Spermatozoa</title><title type="shortAuthors">M Słowińska and A Ciereszko</title><title type="short">Acrosin II of Turkey Spermatozoa</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#aff-1-1"><personName><givenNames>M</givenNames><familyName>Słowińska</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#aff-1-1"><personName><givenNames>A</givenNames><familyName>Ciereszko</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="aff-1-1" countryCode="PL"><unparsedAffiliation>Department of Gamete and Embryo Biology, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences in Olsztyn, Tuwima, Olsztyn, Poland</unparsedAffiliation></affiliation></affiliationGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Contents</title><p>Acrosin from turkey spermatozoa has been recently identified and characterized. In this study, we reported the identification of second form of acrosin (acrosin II) in turkey spermatozoa. Using the three‐step isolation procedure, we purified and characterized the acrosin II from a turkey spermatozoa extract. N‐terminal Edman sequencing allowed the identification of the 24 amino acids from the internal part of acrosin II: SLQEYVEPYRVLQEAKVQLIDLNL. Thanks to homology alignment, we concluded that acrosin II is an acrosin‐like protein similar to avian acrosin, including turkey acrosin. The molecular mass of acrosin II estimated by mass spectrometry was 30.869 kDa. During chromatofocusing, the acrosin II was eluted at pH range from 6.4 to 6.2. Acrosin II was found to be a glycoprotein. The glucosamine and galactosamine were present in carbohydrate structures of acrosin II. Acrosin II is characterized by similar physicochemical characteristics like previously identified bird acrosins, including acrosin from turkey spermatozoa. Similarities between turkey acrosins were also confirmed immunologically by western blot analysis. It can be suggested that two forms of serine proteinase similar to acrosin exist in turkey spermatozoa. These phenomena of both acrosins in spermatozoa agree with the concept of functional redundancy of proteolytic enzymes in the reproductive system. These redundancies may be important for efficient fertilization in turkey.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1"><p>Comercial feed ‘Golpasz’, Poland.</p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Identification of the Second Form of Acrosin in Turkey Spermatozoa</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Acrosin II of Turkey Spermatozoa</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Identification of the Second Form of Acrosin in Turkey Spermatozoa</title></titleInfo><name type="personal"><namePart type="given">M</namePart><namePart type="family">Słowińska</namePart><affiliation>Department of Gamete and Embryo Biology, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences in Olsztyn, Tuwima, Olsztyn, Poland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A</namePart><namePart type="family">Ciereszko</namePart><affiliation>Department of Gamete and Embryo Biology, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences in Olsztyn, Tuwima, Olsztyn, Poland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">2012-10</dateIssued><edition>Submitted: 21 May 2011; Accepted: 15 Dec 2011</edition><copyrightDate encoding="w3cdtf">2012</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">5</extent></physicalDescription><abstract lang="en">Acrosin from turkey spermatozoa has been recently identified and characterized. In this study, we reported the identification of second form of acrosin (acrosin II) in turkey spermatozoa. Using the three‐step isolation procedure, we purified and characterized the acrosin II from a turkey spermatozoa extract. N‐terminal Edman sequencing allowed the identification of the 24 amino acids from the internal part of acrosin II: SLQEYVEPYRVLQEAKVQLIDLNL. Thanks to homology alignment, we concluded that acrosin II is an acrosin‐like protein similar to avian acrosin, including turkey acrosin. The molecular mass of acrosin II estimated by mass spectrometry was 30.869 kDa. During chromatofocusing, the acrosin II was eluted at pH range from 6.4 to 6.2. Acrosin II was found to be a glycoprotein. The glucosamine and galactosamine were present in carbohydrate structures of acrosin II. Acrosin II is characterized by similar physicochemical characteristics like previously identified bird acrosins, including acrosin from turkey spermatozoa. Similarities between turkey acrosins were also confirmed immunologically by western blot analysis. It can be suggested that two forms of serine proteinase similar to acrosin exist in turkey spermatozoa. These phenomena of both acrosins in spermatozoa agree with the concept of functional redundancy of proteolytic enzymes in the reproductive system. These redundancies may be important for efficient fertilization in turkey.</abstract><relatedItem type="host"><titleInfo><title>Reproduction in Domestic Animals</title></titleInfo><genre type="journal">journal</genre><identifier type="ISSN">0936-6768</identifier><identifier type="eISSN">1439-0531</identifier><identifier type="DOI">10.1111/(ISSN)1439-0531</identifier><identifier type="PublisherID">RDA</identifier><part><date>2012</date><detail type="volume"><caption>vol.</caption><number>47</number></detail><detail type="issue"><caption>no.</caption><number>5</number></detail><extent unit="pages"><start>849</start><end>855</end><total>7</total></extent></part></relatedItem><identifier type="istex">AF8FC289B6270429602559B82FA3119BB0094557</identifier><identifier type="DOI">10.1111/j.1439-0531.2011.01981.x</identifier><identifier type="ArticleID">RDA1981</identifier><accessCondition type="use and reproduction" contentType="copyright">© 2012 Blackwell Verlag GmbH</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Blackwell Publishing Ltd</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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