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J. Biochem, 1994, Vol. 115, No. 3 552-556
© 1994 Japanese Biochemical Society

research-article

Isolation and Properties of a Protein Complex Containing Flagellar Movement-Initiating Phosphoprotein from Testes of a White Salmon

Zong Xuan Jin*, Tetsuo Nakajima*, Masaaki Morisawa** and Hiroshi Hayashi*

*Sugashima Marine Biological Laboratory, School of Science, Nagoya University Sugashima, Toba, Mie 517
**Misaku Marine Biological Laboratory, School of Science, The University of Tokyo Miura, Kanagawa 238-02

Phosphorylation of a tyrosine residue within a 15-kDa protein has been found to play a role in the initiation of flagellar movement of quiescent spermatozoa of the rainbow trout, Salmo gairdneri [Morisawa & Hayashi (1986) Biomed. Res. 6, 181–184; Hayashi et al. (1987) J. Biol. Chem. 262, 16692–16698]. In order to find a more accessible source of the 15-kDa protein for biochemical studies, phosphorylation of proteins was studied in other organs from other species. Cell-free extracts from spermatozoa and testes of Salmonidae were prepared and all catalyzed the cAMP-dependent, Mg2+-requiring, but Ca2+-independent phosphorylation of the 15-kDa proteins. Protein from the testes of a white salmon, Oncorhynchus keta, was isolated by conventional purification methods. The 15-kDa protein in the cell-free extract was found to be complexed with several other proteins such that the 15-kDa protein and its phosphorylating activity were copurified. Isolation of a sufficient amount of the complex for the preparation of antibodies against the various constituents is now possible.


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