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M r 25 000 protein, a substrate for protein serine/threonine kinases, is identified as a part of Xenopus laevis vitellogenin B1
Author(s) -
Yoshitome Satoshi,
Nakamura Hiroyasu,
Nakajo Nobushige,
Okamoto Kengo,
Sugimoto Isamu,
Kohara Hiromi,
Kitayama Kaori,
Igarashi Kazuaki,
Ito Susumu,
Sagata Noriyuki,
Hashimoto Eikichi
Publication year - 2003
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1046/j.1524-4725.2003.696.x
Subject(s) - vitellogenin , xenopus , phosvitin , complementary dna , biology , threonine , protein kinase a , phosphorylation , serine , kinase , casein kinase 1 , yolk , microbiology and biotechnology , cytosol , biochemistry , gene , enzyme , ecology
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 nutrient source, but it might also play a role in rapid development.