Mr 25 000 protein, a substrate for protein serine/threonine kinases, is identified as a part of Xenopus laevis vitellogenin B1

Satoshi Yoshitome, Hiroyasu Nakamura, Nobushige Nakajo, Kengo Okamoto, Isamu Sugimoto, Hiromi Kohara, Kaori Kitayama, Kazuaki Igarashi, Susumu Ito, Noriyuki Sagata, Eikichi Hashimoto

研究成果: ジャーナルへの寄稿学術誌査読

14 被引用数 (Scopus)

抄録

A phosphorylated protein with a molecular mass of 25 000 (pp25) previously purified from the cytosolic fraction of Xenopus laevis oocytes is an effective phosphate acceptor for casein kinases and protein kinase C. In this study, based on the partial amino acid sequence of pp25, a cDNA was isolated that encodes a new yolk precursor protein, Xenopus vitellogenin B1, which contained the sequence encoding pp25. Both mRNA and protein of vitellogenin B1 were expressed in all of the female organs examined. In agreement with a previous report, the amount of vitellogenin B1 protein in the liver increased after stimulation with estrogen. These results suggest that pp25 is a cytosolic non-crystallized yolk protein nutnent source, but it might also play a role in rapid development.

本文言語英語
ページ(範囲)283-294
ページ数12
ジャーナルDevelopment Growth and Differentiation
45
3
DOI
出版ステータス出版済み - 6月 2003

!!!All Science Journal Classification (ASJC) codes

  • 発生生物学
  • 細胞生物学

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