Purification and characterization of maturation-promoting factor in fish
Identifieur interne : 000E96 ( Istex/Corpus ); précédent : 000E95; suivant : 000E97Purification and characterization of maturation-promoting factor in fish
Auteurs : M. Yamashita ; S. Fukada ; M. Yoshikuni ; P. Bulet ; T. Hirai ; A. Yamaguchi ; Y.-H. Lou ; Z. Zhao ; Y. NagahamaSource :
- Developmental Biology [ 0012-1606 ] ; 1992.
Abstract
Maturation-promoting factor (MPF) activity has been demonstrated for the first time in fish oocytes. We purified MPF from a 100,000g supernatant of crushed, naturally spawned carp oocytes using four chromatography columns: Q-Sepharose Fast-Flow, p13sucl-affinity Sepharose, Mono S, and Superose 12. The final preparation was purified over 1000-fold with a recovery of about 1%. On Superose 12, MPF eluted as a single peak with an apparent molecular weight of 100 kDa. SDS-PAGE analysis of the active fractions after Superose 12 revealed the presence of four proteins of 33, 34, 46, and 48 kDa. A monoclonal antibody against the PSTAIR sequence of cdc2 kinase recognized the 33- and 34-kDa proteins for which the 46- and 48-kDa proteins are endogenous substrates. The 46- and 48-kDa proteins were recognized by a monoclonal antibody against Escherichia coli-produced goldfish cyclin B, but not by an anti-cyclin A antibody. When oocytes were matured in the presence of 32P, the labeling was seen with the 34-kDa protein, but not with the 33-kDa protein. The 34-kDa protein corresponded to the MPF activity, but the 33-kDa protein did not. These findings indicate that carp MPF is a complex of cdc2 kinase and cyclin B, and further that active MPF contains the phosphorylated form of cdc2 kinase.
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DOI: 10.1016/0012-1606(92)90259-J
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Yoshikuni</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Bulet, P" sort="Bulet, P" uniqKey="Bulet P" first="P." last="Bulet">P. Bulet</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Hirai, T" sort="Hirai, T" uniqKey="Hirai T" first="T." last="Hirai">T. Hirai</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Yamaguchi, A" sort="Yamaguchi, A" uniqKey="Yamaguchi A" first="A." last="Yamaguchi">A. Yamaguchi</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Lou, Y H" sort="Lou, Y H" uniqKey="Lou Y" first="Y.-H." last="Lou">Y.-H. Lou</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Zhao, Z" sort="Zhao, Z" uniqKey="Zhao Z" first="Z." last="Zhao">Z. Zhao</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Nagahama, Y" sort="Nagahama, Y" uniqKey="Nagahama Y" first="Y." last="Nagahama">Y. 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Yamashita</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Fukada, S" sort="Fukada, S" uniqKey="Fukada S" first="S." last="Fukada">S. Fukada</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Yoshikuni, M" sort="Yoshikuni, M" uniqKey="Yoshikuni M" first="M." last="Yoshikuni">M. Yoshikuni</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Bulet, P" sort="Bulet, P" uniqKey="Bulet P" first="P." last="Bulet">P. Bulet</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Hirai, T" sort="Hirai, T" uniqKey="Hirai T" first="T." last="Hirai">T. Hirai</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Yamaguchi, A" sort="Yamaguchi, A" uniqKey="Yamaguchi A" first="A." last="Yamaguchi">A. Yamaguchi</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Lou, Y H" sort="Lou, Y H" uniqKey="Lou Y" first="Y.-H." last="Lou">Y.-H. Lou</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Zhao, Z" sort="Zhao, Z" uniqKey="Zhao Z" first="Z." last="Zhao">Z. Zhao</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author><author><name sortKey="Nagahama, Y" sort="Nagahama, Y" uniqKey="Nagahama Y" first="Y." last="Nagahama">Y. Nagahama</name><affiliation><mods:affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Developmental Biology</title><title level="j" type="abbrev">YDBIO</title><idno type="ISSN">0012-1606</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1992">1992</date><biblScope unit="volume">149</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="8">8</biblScope><biblScope unit="page" to="15">15</biblScope></imprint><idno type="ISSN">0012-1606</idno></series><idno type="istex">899661E27E06F58AE6132B8479005F7EC56CA4BC</idno><idno type="DOI">10.1016/0012-1606(92)90259-J</idno><idno type="PII">0012-1606(92)90259-J</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0012-1606</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Maturation-promoting factor (MPF) activity has been demonstrated for the first time in fish oocytes. We purified MPF from a 100,000g supernatant of crushed, naturally spawned carp oocytes using four chromatography columns: Q-Sepharose Fast-Flow, p13sucl-affinity Sepharose, Mono S, and Superose 12. The final preparation was purified over 1000-fold with a recovery of about 1%. On Superose 12, MPF eluted as a single peak with an apparent molecular weight of 100 kDa. SDS-PAGE analysis of the active fractions after Superose 12 revealed the presence of four proteins of 33, 34, 46, and 48 kDa. A monoclonal antibody against the PSTAIR sequence of cdc2 kinase recognized the 33- and 34-kDa proteins for which the 46- and 48-kDa proteins are endogenous substrates. The 46- and 48-kDa proteins were recognized by a monoclonal antibody against Escherichia coli-produced goldfish cyclin B, but not by an anti-cyclin A antibody. When oocytes were matured in the presence of 32P, the labeling was seen with the 34-kDa protein, but not with the 33-kDa protein. The 34-kDa protein corresponded to the MPF activity, but the 33-kDa protein did not. These findings indicate that carp MPF is a complex of cdc2 kinase and cyclin B, and further that active MPF contains the phosphorylated form of cdc2 kinase.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>M. Yamashita</name><affiliations><json:string>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</json:string></affiliations></json:item><json:item><name>S. Fukada</name><affiliations><json:string>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</json:string></affiliations></json:item><json:item><name>M. Yoshikuni</name><affiliations><json:string>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</json:string></affiliations></json:item><json:item><name>P. Bulet</name><affiliations><json:string>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</json:string></affiliations></json:item><json:item><name>T. Hirai</name><affiliations><json:string>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</json:string></affiliations></json:item><json:item><name>A. Yamaguchi</name><affiliations><json:string>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</json:string></affiliations></json:item><json:item><name>Y.-H. Lou</name><affiliations><json:string>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</json:string></affiliations></json:item><json:item><name>Z. Zhao</name><affiliations><json:string>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</json:string></affiliations></json:item><json:item><name>Y. Nagahama</name><affiliations><json:string>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</json:string></affiliations></json:item></author><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Maturation-promoting factor (MPF) activity has been demonstrated for the first time in fish oocytes. We purified MPF from a 100,000g supernatant of crushed, naturally spawned carp oocytes using four chromatography columns: Q-Sepharose Fast-Flow, p13sucl-affinity Sepharose, Mono S, and Superose 12. The final preparation was purified over 1000-fold with a recovery of about 1%. On Superose 12, MPF eluted as a single peak with an apparent molecular weight of 100 kDa. SDS-PAGE analysis of the active fractions after Superose 12 revealed the presence of four proteins of 33, 34, 46, and 48 kDa. A monoclonal antibody against the PSTAIR sequence of cdc2 kinase recognized the 33- and 34-kDa proteins for which the 46- and 48-kDa proteins are endogenous substrates. The 46- and 48-kDa proteins were recognized by a monoclonal antibody against Escherichia coli-produced goldfish cyclin B, but not by an anti-cyclin A antibody. When oocytes were matured in the presence of 32P, the labeling was seen with the 34-kDa protein, but not with the 33-kDa protein. The 34-kDa protein corresponded to the MPF activity, but the 33-kDa protein did not. These findings indicate that carp MPF is a complex of cdc2 kinase and cyclin B, and further that active MPF contains the phosphorylated form of cdc2 kinase.</abstract><qualityIndicators><score>7.31</score><pdfVersion>1.3</pdfVersion><pdfPageSize>612.28 x 792 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>0</keywordCount><abstractCharCount>1294</abstractCharCount><pdfWordCount>4838</pdfWordCount><pdfCharCount>30789</pdfCharCount><pdfPageCount>8</pdfPageCount><abstractWordCount>206</abstractWordCount></qualityIndicators><title>Purification and characterization of maturation-promoting factor in fish</title><pii><json:string>0012-1606(92)90259-J</json:string></pii><genre><json:string>research-article</json:string></genre><serie><volume>86</volume><pages><last>4366</last><first>4362</first></pages><language><json:string>unknown</json:string></language><title>Proc. Natl. Acad. Sci. 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biology</json:string></scienceMetrix></categories><publicationDate>1992</publicationDate><copyrightDate>1992</copyrightDate><doi><json:string>10.1016/0012-1606(92)90259-J</json:string></doi><id>899661E27E06F58AE6132B8479005F7EC56CA4BC</id><score>0.02343923</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/899661E27E06F58AE6132B8479005F7EC56CA4BC/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/899661E27E06F58AE6132B8479005F7EC56CA4BC/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/899661E27E06F58AE6132B8479005F7EC56CA4BC/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a">Purification and characterization of maturation-promoting factor in fish</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1992</date></publicationStmt><notesStmt><note>This work was supported by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan (0120210 to Y.N.), the Naito Foundation, and the Japan Health Sciences Foundation.</note><note type="content">Section title: Full paper</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Purification and characterization of maturation-promoting factor in fish</title><author xml:id="author-1"><persName><forename type="first">M.</forename><surname>Yamashita</surname></persName><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation></author><author xml:id="author-2"><persName><forename type="first">S.</forename><surname>Fukada</surname></persName><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation></author><author xml:id="author-3"><persName><forename type="first">M.</forename><surname>Yoshikuni</surname></persName><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation></author><author xml:id="author-4"><persName><forename type="first">P.</forename><surname>Bulet</surname></persName><note type="biography">Current address: Laboratoire de Biologie Generale, Universite Louis Pasteur, CNRS URA 672, Strasbourg 67000, France.</note><affiliation>Current address: Laboratoire de Biologie Generale, Universite Louis Pasteur, CNRS URA 672, Strasbourg 67000, France.</affiliation><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation></author><author xml:id="author-5"><persName><forename type="first">T.</forename><surname>Hirai</surname></persName><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation></author><author xml:id="author-6"><persName><forename type="first">A.</forename><surname>Yamaguchi</surname></persName><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation></author><author xml:id="author-7"><persName><forename type="first">Y.-H.</forename><surname>Lou</surname></persName><note type="biography">Current address: Clinical Immunology Laboratory, Division of Laboratory Medicine, Washington University School of Medicine, St. Louis, MO 63110.</note><affiliation>Current address: Clinical Immunology Laboratory, Division of Laboratory Medicine, Washington University School of Medicine, St. Louis, MO 63110.</affiliation><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation></author><author xml:id="author-8"><persName><forename type="first">Z.</forename><surname>Zhao</surname></persName><note type="biography">Current address: Department of Cell and Structural Biology, University of Manchester, Oxford Road, Manchester M13 9PT, UK.</note><affiliation>Current address: Department of Cell and Structural Biology, University of Manchester, Oxford Road, Manchester M13 9PT, UK.</affiliation><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation></author><author xml:id="author-9"><persName><forename type="first">Y.</forename><surname>Nagahama</surname></persName><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation></author></analytic><monogr><title level="j">Developmental Biology</title><title level="j" type="abbrev">YDBIO</title><idno type="pISSN">0012-1606</idno><idno type="PII">S0012-1606(00)X0568-4</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1992"></date><biblScope unit="volume">149</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="8">8</biblScope><biblScope unit="page" to="15">15</biblScope></imprint></monogr><idno type="istex">899661E27E06F58AE6132B8479005F7EC56CA4BC</idno><idno type="DOI">10.1016/0012-1606(92)90259-J</idno><idno type="PII">0012-1606(92)90259-J</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1992</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Maturation-promoting factor (MPF) activity has been demonstrated for the first time in fish oocytes. We purified MPF from a 100,000g supernatant of crushed, naturally spawned carp oocytes using four chromatography columns: Q-Sepharose Fast-Flow, p13sucl-affinity Sepharose, Mono S, and Superose 12. The final preparation was purified over 1000-fold with a recovery of about 1%. On Superose 12, MPF eluted as a single peak with an apparent molecular weight of 100 kDa. SDS-PAGE analysis of the active fractions after Superose 12 revealed the presence of four proteins of 33, 34, 46, and 48 kDa. A monoclonal antibody against the PSTAIR sequence of cdc2 kinase recognized the 33- and 34-kDa proteins for which the 46- and 48-kDa proteins are endogenous substrates. The 46- and 48-kDa proteins were recognized by a monoclonal antibody against Escherichia coli-produced goldfish cyclin B, but not by an anti-cyclin A antibody. When oocytes were matured in the presence of 32P, the labeling was seen with the 34-kDa protein, but not with the 33-kDa protein. The 34-kDa protein corresponded to the MPF activity, but the 33-kDa protein did not. These findings indicate that carp MPF is a complex of cdc2 kinase and cyclin B, and further that active MPF contains the phosphorylated form of cdc2 kinase.</p></abstract></profileDesc><revisionDesc><change when="1992">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/899661E27E06F58AE6132B8479005F7EC56CA4BC/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>YDBIO</jid><aid>9290259J</aid><ce:pii>0012-1606(92)90259-J</ce:pii><ce:doi>10.1016/0012-1606(92)90259-J</ce:doi><ce:copyright type="unknown" year="1992"></ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>This work was supported by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan (0120210 to Y.N.), the Naito Foundation, and the Japan Health Sciences Foundation.</ce:note-para></ce:article-footnote><ce:dochead><ce:textfn>Full paper</ce:textfn></ce:dochead><ce:title>Purification and characterization of maturation-promoting factor in fish</ce:title><ce:author-group><ce:author><ce:given-name>M.</ce:given-name><ce:surname>Yamashita</ce:surname></ce:author><ce:author><ce:given-name>S.</ce:given-name><ce:surname>Fukada</ce:surname></ce:author><ce:author><ce:given-name>M.</ce:given-name><ce:surname>Yoshikuni</ce:surname></ce:author><ce:author><ce:given-name>P.</ce:given-name><ce:surname>Bulet</ce:surname><ce:cross-ref refid="FN1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>T.</ce:given-name><ce:surname>Hirai</ce:surname></ce:author><ce:author><ce:given-name>A.</ce:given-name><ce:surname>Yamaguchi</ce:surname></ce:author><ce:author><ce:given-name>Y.-H.</ce:given-name><ce:surname>Lou</ce:surname><ce:cross-ref refid="FN2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Z.</ce:given-name><ce:surname>Zhao</ce:surname><ce:cross-ref refid="FN3"><ce:sup>3</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Y.</ce:given-name><ce:surname>Nagahama</ce:surname></ce:author><ce:affiliation><ce:textfn>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</ce:textfn></ce:affiliation><ce:footnote id="FN1"><ce:label>1</ce:label><ce:note-para>Current address: Laboratoire de Biologie Generale, Universite Louis Pasteur, CNRS URA 672, Strasbourg 67000, France.</ce:note-para></ce:footnote><ce:footnote id="FN2"><ce:label>2</ce:label><ce:note-para>Current address: Clinical Immunology Laboratory, Division of Laboratory Medicine, Washington University School of Medicine, St. Louis, MO 63110.</ce:note-para></ce:footnote><ce:footnote id="FN3"><ce:label>3</ce:label><ce:note-para>Current address: Department of Cell and Structural Biology, University of Manchester, Oxford Road, Manchester M13 9PT, UK.</ce:note-para></ce:footnote></ce:author-group><ce:date-accepted day="9" month="9" year="1991"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Maturation-promoting factor (MPF) activity has been demonstrated for the first time in fish oocytes. We purified MPF from a 100,000<ce:italic>g</ce:italic> supernatant of crushed, naturally spawned carp oocytes using four chromatography columns: Q-Sepharose Fast-Flow, p13<ce:sup>sucl</ce:sup>-affinity Sepharose, Mono S, and Superose 12. The final preparation was purified over 1000-fold with a recovery of about 1%. On Superose 12, MPF eluted as a single peak with an apparent molecular weight of 100 kDa. SDS-PAGE analysis of the active fractions after Superose 12 revealed the presence of four proteins of 33, 34, 46, and 48 kDa. A monoclonal antibody against the PSTAIR sequence of cdc2 kinase recognized the 33- and 34-kDa proteins for which the 46- and 48-kDa proteins are endogenous substrates. The 46- and 48-kDa proteins were recognized by a monoclonal antibody against <ce:italic>Escherichia coli</ce:italic>-produced goldfish cyclin B, but not by an anti-cyclin A antibody. When oocytes were matured in the presence of <ce:sup loc="pre">32</ce:sup>P, the labeling was seen with the 34-kDa protein, but not with the 33-kDa protein. The 34-kDa protein corresponded to the MPF activity, but the 33-kDa protein did not. These findings indicate that carp MPF is a complex of cdc2 kinase and cyclin B, and further that active MPF contains the phosphorylated form of cdc2 kinase.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Purification and characterization of maturation-promoting factor in fish</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Purification and characterization of maturation-promoting factor in fish</title></titleInfo><name type="personal"><namePart type="given">M.</namePart><namePart type="family">Yamashita</namePart><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.</namePart><namePart type="family">Fukada</namePart><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.</namePart><namePart type="family">Yoshikuni</namePart><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">P.</namePart><namePart type="family">Bulet</namePart><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation><description>Current address: Laboratoire de Biologie Generale, Universite Louis Pasteur, CNRS URA 672, Strasbourg 67000, France.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">T.</namePart><namePart type="family">Hirai</namePart><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.</namePart><namePart type="family">Yamaguchi</namePart><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Y.-H.</namePart><namePart type="family">Lou</namePart><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation><description>Current address: Clinical Immunology Laboratory, Division of Laboratory Medicine, Washington University School of Medicine, St. Louis, MO 63110.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Z.</namePart><namePart type="family">Zhao</namePart><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation><description>Current address: Department of Cell and Structural Biology, University of Manchester, Oxford Road, Manchester M13 9PT, UK.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Y.</namePart><namePart type="family">Nagahama</namePart><affiliation>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1992</dateIssued><copyrightDate encoding="w3cdtf">1992</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">Maturation-promoting factor (MPF) activity has been demonstrated for the first time in fish oocytes. We purified MPF from a 100,000g supernatant of crushed, naturally spawned carp oocytes using four chromatography columns: Q-Sepharose Fast-Flow, p13sucl-affinity Sepharose, Mono S, and Superose 12. The final preparation was purified over 1000-fold with a recovery of about 1%. On Superose 12, MPF eluted as a single peak with an apparent molecular weight of 100 kDa. SDS-PAGE analysis of the active fractions after Superose 12 revealed the presence of four proteins of 33, 34, 46, and 48 kDa. A monoclonal antibody against the PSTAIR sequence of cdc2 kinase recognized the 33- and 34-kDa proteins for which the 46- and 48-kDa proteins are endogenous substrates. The 46- and 48-kDa proteins were recognized by a monoclonal antibody against Escherichia coli-produced goldfish cyclin B, but not by an anti-cyclin A antibody. When oocytes were matured in the presence of 32P, the labeling was seen with the 34-kDa protein, but not with the 33-kDa protein. The 34-kDa protein corresponded to the MPF activity, but the 33-kDa protein did not. These findings indicate that carp MPF is a complex of cdc2 kinase and cyclin B, and further that active MPF contains the phosphorylated form of cdc2 kinase.</abstract><note>This work was supported by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan (0120210 to Y.N.), the Naito Foundation, and the Japan Health Sciences Foundation.</note><note type="content">Section title: Full paper</note><relatedItem type="host"><titleInfo><title>Developmental Biology</title></titleInfo><titleInfo type="abbreviated"><title>YDBIO</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">199201</dateIssued></originInfo><identifier type="ISSN">0012-1606</identifier><identifier type="PII">S0012-1606(00)X0568-4</identifier><part><date>199201</date><detail type="volume"><number>149</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>237</end></extent><extent unit="pages"><start>8</start><end>15</end></extent></part></relatedItem><identifier type="istex">899661E27E06F58AE6132B8479005F7EC56CA4BC</identifier><identifier type="DOI">10.1016/0012-1606(92)90259-J</identifier><identifier type="PII">0012-1606(92)90259-J</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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