J. Biochem, 2003, Vol. 133, No. 3 361-369
© 2003 Japanese Biochemical Society
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Identification of 36-kDa Flagellar Phosphoproteins Associated with Hamster Sperm Motility
1 Department of Physiology, Dokkyo University School of Medicine, Mibu, Tochigi 321-0293; 2 Department of Molecular Biology, Keio University School of Medicine, Shinanomachi, Shinjuku-ku, Tokyo 160-8582; 3 TMIG Proteomics Collaboration Center, Tokyo Metropolitan Institute of Gerontology, Sakaecho, Itabashi-ku, Tokyo 173-0015; 4 Department of Biology, Tokyo Gakugei University, Koganei, Tokyo 184-8501; and 5 Department of Biology, Graduate School of Arts and Science, University of Tokyo, Komaba, Meguro-ku, Tokyo 153-0041
In our previous paper [M. Fujinoki et al. (2001) Biomed. Res. 22, 45–58], we reported that two types of 36-kDa protein, which were designated as 36K-A protein and 36K-B protein, obtained from hamster sperm flagella were phosphorylated at serine residues associated with the regulation of motility activation. In the present experiments, it was suggested that these two types of 36-kDa protein were phosphorylated in a cAMP-dependent manner associated with motility activation of hamster spermatozoa. Because the 36K-B protein was the most intensely phosphorylated in a cAMP-dependent manner, attempts were made to further characterize it. The 36K-B protein was assumed to be localized in the middle piece. The localization of the 36K-B protein was the same as that of the 36-kDa protein reported in our previous paper [Y. Si et al. (1999) Mol. Reprod. Dev. 52, 328–334]. In order to identify the 36K-B protein, it was analyzed by peptide mass finger printing and amino acid sequencing. The results suggested that the 36K-B protein was a pyruvate dehydrogenase E1 component ß subunit and a component of the mitochondrial sheath of the middle piece.
+ To whom correspondence should be addressed. Tel: +81-282-87-2125, Fax: +81-282-86-7835, E-mail: fujinoki{at}dokkyomed.ac.jp
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