Serine proteinase inhibitors of seminal plasma of teleost fish: distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood
Identifieur interne : 000102 ( Istex/Corpus ); précédent : 000101; suivant : 000103Serine proteinase inhibitors of seminal plasma of teleost fish: distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood
Auteurs : A. Ciereszko ; B. Piros ; K. Dabrowski ; D. Kucharczyk ; M. J. Łuczy Ski ; S. Dobosz ; J. GlogowskiSource :
- Journal of Fish Biology [ 0022-1112 ] ; 1998-12.
English descriptors
- KwdEn :
Abstract
Anti‐proteinase activity has been found in seminal plasma of eight teleost fish species: brown trout, rainbow trout, brook trout, lake whitefish, bream, northern pike, Danube salmon and burbot. This activity correlated with seminal plasma protein and sperm concentrations. Using a mammalian (bovine) trypsin for detecting proteinase inhibitors it was found for the first time that there are species‐specific electrophoretic profiles of anti‐proteinase activity. One to three bands could be identified by this method. However, additional proteinase inhibitors could be identified by using fish (cod) trypsin. These inhibitors were detected in seminal plasma of salmonids and coregonids and have a slow migration rate. Fast‐migrating proteinase inhibitors were present in rainbow, brown and brook trout, northern pike, whitefish and burbot. These inhibitors could be detected in brook and brown trout by using either trypsins. However, they were detected only with bovine trypsin in rainbow trout, northern pike, whitefish and burbot. These results suggest that multiple forms of serine proteinase inhibitors exist in seminal plasma of teleost fish and they differ in their affinity toward serine proteinases. Seminal plasma serine proteinase inhibitors of rainbow trout migrated during electrophoresis similarly to blood plasma proteinase inhibitors, and suggests that the two inhibitors may be similar or the same. Anti‐proteinase specific activity was similar in blood and seminal plasma. Proteinase inhibitors of fish seminal plasma seem to be an important part of sperm physiology, possibly related to protection of spermatozoa. Staining for detection of serine proteinase inhibitors also allowed detection of presence of nonspecific esterase in seminal plasma of most species.
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DOI: 10.1111/j.1095-8649.1998.tb00249.x
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ISTEX:5261C45A351037CF6A585F0B55D468D8A6D213D4Le document en format XML
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Piros</name><affiliation><mods:affiliation>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</mods:affiliation></affiliation></author><author><name sortKey="Dabrowski, K" sort="Dabrowski, K" uniqKey="Dabrowski K" first="K." last="Dabrowski">K. Dabrowski</name><affiliation><mods:affiliation>School of Natural Resources, The Ohio State University, 210 Kottman Hall, 2021 Coffey Rd, Columbus, OH 43210, U.S.A.</mods:affiliation></affiliation></author><author><name sortKey="Kucharczyk, D" sort="Kucharczyk, D" uniqKey="Kucharczyk D" first="D." last="Kucharczyk">D. Kucharczyk</name><affiliation><mods:affiliation>Department of Fisheries, Olsztyn University of Agriculture and Technology, Oczapowskiego 5, 10‐718 Olsztyn‐Kortowo, Poland</mods:affiliation></affiliation></author><author><name sortKey="Luczy Ski, M J" sort="Luczy Ski, M J" uniqKey="Luczy Ski M" first="M. J." last="Łuczy Ski">M. J. 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Ciereszko</name><affiliation><mods:affiliation>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</mods:affiliation></affiliation></author><author><name sortKey="Piros, B" sort="Piros, B" uniqKey="Piros B" first="B." last="Piros">B. Piros</name><affiliation><mods:affiliation>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</mods:affiliation></affiliation></author><author><name sortKey="Dabrowski, K" sort="Dabrowski, K" uniqKey="Dabrowski K" first="K." last="Dabrowski">K. Dabrowski</name><affiliation><mods:affiliation>School of Natural Resources, The Ohio State University, 210 Kottman Hall, 2021 Coffey Rd, Columbus, OH 43210, U.S.A.</mods:affiliation></affiliation></author><author><name sortKey="Kucharczyk, D" sort="Kucharczyk, D" uniqKey="Kucharczyk D" first="D." last="Kucharczyk">D. Kucharczyk</name><affiliation><mods:affiliation>Department of Fisheries, Olsztyn University of Agriculture and Technology, Oczapowskiego 5, 10‐718 Olsztyn‐Kortowo, Poland</mods:affiliation></affiliation></author><author><name sortKey="Luczy Ski, M J" sort="Luczy Ski, M J" uniqKey="Luczy Ski M" first="M. J." last="Łuczy Ski">M. J. Łuczy Ski</name><affiliation><mods:affiliation>Inland Fisheries Institut, czapowskiego 10, 10‐718 Olsztyn‐Kortowo, Poland</mods:affiliation></affiliation></author><author><name sortKey="Dobosz, S" sort="Dobosz, S" uniqKey="Dobosz S" first="S." last="Dobosz">S. Dobosz</name><affiliation><mods:affiliation>Salmonid Research Laboratory, Inland Fisheries Institute, Rutki, 83‐330 Zukowo, Poland</mods:affiliation></affiliation></author><author><name sortKey="Glogowski, J" sort="Glogowski, J" uniqKey="Glogowski J" first="J." last="Glogowski">J. Glogowski</name><affiliation><mods:affiliation>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Fish Biology</title><idno type="ISSN">0022-1112</idno><idno type="eISSN">1095-8649</idno><imprint><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1998-12">1998-12</date><biblScope unit="volume">53</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="1292">1292</biblScope><biblScope unit="page" to="1305">1305</biblScope></imprint><idno type="ISSN">0022-1112</idno></series><idno type="istex">5261C45A351037CF6A585F0B55D468D8A6D213D4</idno><idno type="DOI">10.1111/j.1095-8649.1998.tb00249.x</idno><idno type="ArticleID">JFB1292</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-1112</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>proteinase inhibitors</term><term>semen</term><term>teleost fish</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Anti‐proteinase activity has been found in seminal plasma of eight teleost fish species: brown trout, rainbow trout, brook trout, lake whitefish, bream, northern pike, Danube salmon and burbot. This activity correlated with seminal plasma protein and sperm concentrations. Using a mammalian (bovine) trypsin for detecting proteinase inhibitors it was found for the first time that there are species‐specific electrophoretic profiles of anti‐proteinase activity. One to three bands could be identified by this method. However, additional proteinase inhibitors could be identified by using fish (cod) trypsin. These inhibitors were detected in seminal plasma of salmonids and coregonids and have a slow migration rate. Fast‐migrating proteinase inhibitors were present in rainbow, brown and brook trout, northern pike, whitefish and burbot. These inhibitors could be detected in brook and brown trout by using either trypsins. However, they were detected only with bovine trypsin in rainbow trout, northern pike, whitefish and burbot. These results suggest that multiple forms of serine proteinase inhibitors exist in seminal plasma of teleost fish and they differ in their affinity toward serine proteinases. Seminal plasma serine proteinase inhibitors of rainbow trout migrated during electrophoresis similarly to blood plasma proteinase inhibitors, and suggests that the two inhibitors may be similar or the same. Anti‐proteinase specific activity was similar in blood and seminal plasma. Proteinase inhibitors of fish seminal plasma seem to be an important part of sperm physiology, possibly related to protection of spermatozoa. Staining for detection of serine proteinase inhibitors also allowed detection of presence of nonspecific esterase in seminal plasma of most species.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>A. Ciereszko</name><affiliations><json:string>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</json:string></affiliations></json:item><json:item><name>B. Piros</name><affiliations><json:string>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</json:string></affiliations></json:item><json:item><name>K. Dabrowski</name><affiliations><json:string>School of Natural Resources, The Ohio State University, 210 Kottman Hall, 2021 Coffey Rd, Columbus, OH 43210, U.S.A.</json:string></affiliations></json:item><json:item><name>D. Kucharczyk</name><affiliations><json:string>Department of Fisheries, Olsztyn University of Agriculture and Technology, Oczapowskiego 5, 10‐718 Olsztyn‐Kortowo, Poland</json:string></affiliations></json:item><json:item><name>M. J. ŁUczyński</name><affiliations><json:string>Inland Fisheries Institut, czapowskiego 10, 10‐718 Olsztyn‐Kortowo, Poland</json:string></affiliations></json:item><json:item><name>S. Dobosz</name><affiliations><json:string>Salmonid Research Laboratory, Inland Fisheries Institute, Rutki, 83‐330 Zukowo, Poland</json:string></affiliations></json:item><json:item><name>J. Glogowski</name><affiliations><json:string>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>teleost fish</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>semen</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>proteinase inhibitors</value></json:item></subject><language><json:string>eng</json:string></language><abstract>Anti‐proteinase activity has been found in seminal plasma of eight teleost fish species: brown trout, rainbow trout, brook trout, lake whitefish, bream, northern pike, Danube salmon and burbot. This activity correlated with seminal plasma protein and sperm concentrations. Using a mammalian (bovine) trypsin for detecting proteinase inhibitors it was found for the first time that there are species‐specific electrophoretic profiles of anti‐proteinase activity. One to three bands could be identified by this method. However, additional proteinase inhibitors could be identified by using fish (cod) trypsin. These inhibitors were detected in seminal plasma of salmonids and coregonids and have a slow migration rate. Fast‐migrating proteinase inhibitors were present in rainbow, brown and brook trout, northern pike, whitefish and burbot. These inhibitors could be detected in brook and brown trout by using either trypsins. However, they were detected only with bovine trypsin in rainbow trout, northern pike, whitefish and burbot. These results suggest that multiple forms of serine proteinase inhibitors exist in seminal plasma of teleost fish and they differ in their affinity toward serine proteinases. Seminal plasma serine proteinase inhibitors of rainbow trout migrated during electrophoresis similarly to blood plasma proteinase inhibitors, and suggests that the two inhibitors may be similar or the same. Anti‐proteinase specific activity was similar in blood and seminal plasma. Proteinase inhibitors of fish seminal plasma seem to be an important part of sperm physiology, possibly related to protection of spermatozoa. 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Fax: +48 89 535 7421; email:</p></note><affiliation>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</affiliation></author><author><persName><forename type="first">B.</forename><surname>Piros</surname></persName><affiliation>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</affiliation></author><author><persName><forename type="first">K.</forename><surname>Dabrowski</surname></persName><affiliation>School of Natural Resources, The Ohio State University, 210 Kottman Hall, 2021 Coffey Rd, Columbus, OH 43210, U.S.A.</affiliation></author><author><persName><forename type="first">D.</forename><surname>Kucharczyk</surname></persName><affiliation>Department of Fisheries, Olsztyn University of Agriculture and Technology, Oczapowskiego 5, 10‐718 Olsztyn‐Kortowo, Poland</affiliation></author><author><persName><forename type="first">M. J.</forename><surname>ŁUczyński</surname></persName><affiliation>Inland Fisheries Institut, czapowskiego 10, 10‐718 Olsztyn‐Kortowo, Poland</affiliation></author><author><persName><forename type="first">S.</forename><surname>Dobosz</surname></persName><affiliation>Salmonid Research Laboratory, Inland Fisheries Institute, Rutki, 83‐330 Zukowo, Poland</affiliation></author><author><persName><forename type="first">J.</forename><surname>Glogowski</surname></persName><affiliation>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</affiliation></author></analytic><monogr><title level="j">Journal of Fish Biology</title><idno type="pISSN">0022-1112</idno><idno type="eISSN">1095-8649</idno><idno type="DOI">10.1111/(ISSN)1095-8649</idno><imprint><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1998-12"></date><biblScope unit="volume">53</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="1292">1292</biblScope><biblScope unit="page" to="1305">1305</biblScope></imprint></monogr><idno type="istex">5261C45A351037CF6A585F0B55D468D8A6D213D4</idno><idno type="DOI">10.1111/j.1095-8649.1998.tb00249.x</idno><idno type="ArticleID">JFB1292</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1998</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Anti‐proteinase activity has been found in seminal plasma of eight teleost fish species: brown trout, rainbow trout, brook trout, lake whitefish, bream, northern pike, Danube salmon and burbot. This activity correlated with seminal plasma protein and sperm concentrations. Using a mammalian (bovine) trypsin for detecting proteinase inhibitors it was found for the first time that there are species‐specific electrophoretic profiles of anti‐proteinase activity. One to three bands could be identified by this method. However, additional proteinase inhibitors could be identified by using fish (cod) trypsin. These inhibitors were detected in seminal plasma of salmonids and coregonids and have a slow migration rate. Fast‐migrating proteinase inhibitors were present in rainbow, brown and brook trout, northern pike, whitefish and burbot. These inhibitors could be detected in brook and brown trout by using either trypsins. However, they were detected only with bovine trypsin in rainbow trout, northern pike, whitefish and burbot. These results suggest that multiple forms of serine proteinase inhibitors exist in seminal plasma of teleost fish and they differ in their affinity toward serine proteinases. Seminal plasma serine proteinase inhibitors of rainbow trout migrated during electrophoresis similarly to blood plasma proteinase inhibitors, and suggests that the two inhibitors may be similar or the same. Anti‐proteinase specific activity was similar in blood and seminal plasma. Proteinase inhibitors of fish seminal plasma seem to be an important part of sperm physiology, possibly related to protection of spermatozoa. Staining for detection of serine proteinase inhibitors also allowed detection of presence of nonspecific esterase in seminal plasma of most species.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>teleost fish</term></item><item><term>semen</term></item><item><term>proteinase inhibitors</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998-12">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/5261C45A351037CF6A585F0B55D468D8A6D213D4/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 version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Blackwell Publishing Ltd</publisherName><publisherLoc>Oxford, UK</publisherLoc></publisherInfo><doi origin="wiley" registered="yes">10.1111/(ISSN)1095-8649</doi><issn type="print">0022-1112</issn><issn type="electronic">1095-8649</issn><idGroup><id type="product" value="JFB"></id><id type="publisherDivision" value="ST"></id></idGroup><titleGroup><title type="main" sort="JOURNAL OF FISH BIOLOGY">Journal of Fish Biology</title></titleGroup></publicationMeta><publicationMeta level="part" position="12006"><doi origin="wiley">10.1111/jfb.1998.53.issue-6</doi><numberingGroup><numbering type="journalVolume" number="53">53</numbering><numbering type="journalIssue" number="6">6</numbering></numberingGroup><coverDate startDate="1998-12">December 1998</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="0129200" status="forIssue"><doi origin="wiley">10.1111/j.1095-8649.1998.tb00249.x</doi><idGroup><id type="unit" value="JFB1292"></id></idGroup><countGroup><count type="pageTotal" number="14"></count></countGroup><eventGroup><event type="firstOnline" date="2005-04-01"></event><event type="publishedOnlineFinalForm" date="2005-04-01"></event><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:2.3.6 mode:FullText source:HeaderRef result:HeaderRef" date="2010-04-20"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-30"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-30"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="1292">1292</numbering><numbering type="pageLast" number="1305">1305</numbering></numberingGroup><correspondenceTo> Author to whom correspondence should be addressed. Fax: +48 89 535 7421; email: <email>acieresz@food.irzbz.pan.olsztyn.pl</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:JFB.JFB1292.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received 14 April 1998, Accepted 1 August 1998</unparsedEditorialHistory><countGroup><count type="referenceTotal" number="37"></count><count type="linksCrossRef" number="8"></count></countGroup><titleGroup><title type="main">Serine proteinase inhibitors of seminal plasma of teleost fish: distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1" corresponding="yes"><personName><givenNames>A.</givenNames><familyName>Ciereszko</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a1"><personName><givenNames>B.</givenNames><familyName>Piros</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a2"><personName><givenNames>K.</givenNames><familyName>Dabrowski</familyName></personName></creator><creator creatorRole="author" xml:id="cr4" affiliationRef="#a3"><personName><givenNames>D.</givenNames><familyName>Kucharczyk</familyName></personName></creator><creator creatorRole="author" xml:id="cr5" affiliationRef="#a4"><personName><givenNames>M. 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This activity correlated with seminal plasma protein and sperm concentrations. Using a mammalian (bovine) trypsin for detecting proteinase inhibitors it was found for the first time that there are species‐specific electrophoretic profiles of anti‐proteinase activity. One to three bands could be identified by this method. However, additional proteinase inhibitors could be identified by using fish (cod) trypsin. These inhibitors were detected in seminal plasma of salmonids and coregonids and have a slow migration rate. Fast‐migrating proteinase inhibitors were present in rainbow, brown and brook trout, northern pike, whitefish and burbot. These inhibitors could be detected in brook and brown trout by using either trypsins. However, they were detected only with bovine trypsin in rainbow trout, northern pike, whitefish and burbot. These results suggest that multiple forms of serine proteinase inhibitors exist in seminal plasma of teleost fish and they differ in their affinity toward serine proteinases. Seminal plasma serine proteinase inhibitors of rainbow trout migrated during electrophoresis similarly to blood plasma proteinase inhibitors, and suggests that the two inhibitors may be similar or the same. Anti‐proteinase specific activity was similar in blood and seminal plasma. Proteinase inhibitors of fish seminal plasma seem to be an important part of sperm physiology, possibly related to protection of spermatozoa. Staining for detection of serine proteinase inhibitors also allowed detection of presence of nonspecific esterase in seminal plasma of most species.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Serine proteinase inhibitors of seminal plasma of teleost fish: distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Serine proteinase inhibitors of seminal plasma of teleost fish: distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood</title></titleInfo><name type="personal"><namePart type="given">A.</namePart><namePart type="family">Ciereszko</namePart><affiliation>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</affiliation><description>Correspondence: Author to whom correspondence should be addressed. Fax: +48 89 535 7421; email: </description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">B.</namePart><namePart type="family">Piros</namePart><affiliation>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">K.</namePart><namePart type="family">Dabrowski</namePart><affiliation>School of Natural Resources, The Ohio State University, 210 Kottman Hall, 2021 Coffey Rd, Columbus, OH 43210, U.S.A.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">D.</namePart><namePart type="family">Kucharczyk</namePart><affiliation>Department of Fisheries, Olsztyn University of Agriculture and Technology, Oczapowskiego 5, 10‐718 Olsztyn‐Kortowo, Poland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M. J.</namePart><namePart type="family">ŁUczyński</namePart><affiliation>Inland Fisheries Institut, czapowskiego 10, 10‐718 Olsztyn‐Kortowo, Poland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.</namePart><namePart type="family">Dobosz</namePart><affiliation>Salmonid Research Laboratory, Inland Fisheries Institute, Rutki, 83‐330 Zukowo, Poland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.</namePart><namePart type="family">Glogowski</namePart><affiliation>Institute of Animal Reproduction and Food Research, Department of Molecular Andrology, Polish Academy of Sciences, 10‐718 Olsztyn‐Kortowo, Poland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article">article</genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">1998-12</dateIssued><edition>Received 14 April 1998, Accepted 1 August 1998</edition><copyrightDate encoding="w3cdtf">1998</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="references">37</extent></physicalDescription><abstract lang="en">Anti‐proteinase activity has been found in seminal plasma of eight teleost fish species: brown trout, rainbow trout, brook trout, lake whitefish, bream, northern pike, Danube salmon and burbot. This activity correlated with seminal plasma protein and sperm concentrations. Using a mammalian (bovine) trypsin for detecting proteinase inhibitors it was found for the first time that there are species‐specific electrophoretic profiles of anti‐proteinase activity. One to three bands could be identified by this method. However, additional proteinase inhibitors could be identified by using fish (cod) trypsin. These inhibitors were detected in seminal plasma of salmonids and coregonids and have a slow migration rate. Fast‐migrating proteinase inhibitors were present in rainbow, brown and brook trout, northern pike, whitefish and burbot. These inhibitors could be detected in brook and brown trout by using either trypsins. However, they were detected only with bovine trypsin in rainbow trout, northern pike, whitefish and burbot. These results suggest that multiple forms of serine proteinase inhibitors exist in seminal plasma of teleost fish and they differ in their affinity toward serine proteinases. Seminal plasma serine proteinase inhibitors of rainbow trout migrated during electrophoresis similarly to blood plasma proteinase inhibitors, and suggests that the two inhibitors may be similar or the same. Anti‐proteinase specific activity was similar in blood and seminal plasma. Proteinase inhibitors of fish seminal plasma seem to be an important part of sperm physiology, possibly related to protection of spermatozoa. Staining for detection of serine proteinase inhibitors also allowed detection of presence of nonspecific esterase in seminal plasma of most species.</abstract><subject lang="en"><genre>Keywords</genre><topic>teleost fish</topic><topic>semen</topic><topic>proteinase inhibitors</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Fish Biology</title></titleInfo><identifier type="ISSN">0022-1112</identifier><identifier type="eISSN">1095-8649</identifier><identifier type="DOI">10.1111/(ISSN)1095-8649</identifier><identifier type="PublisherID">JFB</identifier><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>53</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>1292</start><end>1305</end><total>14</total></extent></part></relatedItem><identifier type="istex">5261C45A351037CF6A585F0B55D468D8A6D213D4</identifier><identifier type="DOI">10.1111/j.1095-8649.1998.tb00249.x</identifier><identifier type="ArticleID">JFB1292</identifier><recordInfo><recordOrigin>Blackwell Publishing Ltd</recordOrigin><recordContentSource>WILEY</recordContentSource></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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