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

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 t...

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Veröffentlicht in:	Development, growth & differentiation growth & differentiation, 2003-06, Vol.45 (3), p.283-294
Hauptverfasser:	Yoshitome, Satoshi, Nakamura, Hiroyasu, Nakajo, Nobushige, Okamoto, Kengo, Sugimoto, Isamu, Kohara, Hiromi, Kitayama, Kaori, Igarashi, Kazuaki, Ito, Susumu, Sagata, Noriyuki, Hashimoto, Eikichi
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Base Sequence Blotting, Western DNA, Complementary - genetics estrogen Estrogens - metabolism Expressed Sequence Tags Female Gene Expression Profiling Molecular Sequence Data oocyte Oocytes - chemistry Protein-Serine-Threonine Kinases - metabolism Proteins - chemistry Proteins - isolation & purification Proteins - metabolism Reverse Transcriptase Polymerase Chain Reaction Sequence Analysis, DNA vitellogenin Vitellogenins - chemistry Vitellogenins - genetics Xenopus laevis Xenopus laevis - genetics yolk protein
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