Purification and characterization of maturation-promoting factor in fish
Identifieur interne : 001D56 ( Main/Merge ); précédent : 001D55; suivant : 001D57Purification and characterization of maturation-promoting factor in fish
Auteurs : M. Yamashita [Japon] ; S. Fukada [Japon] ; M. Yoshikuni [Japon] ; P. Bulet [Japon] ; T. Hirai [Japon] ; A. Yamaguchi [Japon] ; Y.-H. Lou [Japon] ; Z. Zhao [Japon] ; Y. Nagahama [Japon]Source :
- 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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Yamashita</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444</wicri:regionArea><wicri:noRegion>Okazaki 444</wicri:noRegion></affiliation></author><author><name sortKey="Fukada, S" sort="Fukada, S" uniqKey="Fukada S" first="S." last="Fukada">S. Fukada</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki 444</wicri:regionArea><wicri:noRegion>Okazaki 444</wicri:noRegion></affiliation></author><author><name sortKey="Yoshikuni, M" sort="Yoshikuni, M" uniqKey="Yoshikuni M" first="M." last="Yoshikuni">M. 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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></record>Pour manipuler ce document sous Unix (Dilib)
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