Isolation and properties of a protein complex containing flagellar movement-initiating phosphoprotein from testes of a white salmon.
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, Mg(2+)-requiring, but Ca(2+)-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.
Jin
Z X
ZX
Sugashima Marine Biological Laboratory, School of Science, Nagoya University, Mie.
Nakajima
T
T
Morisawa
M
M
Hayashi
H
H
D000818:Animals; D002118:Calcium / Q000378:metabolism; D002846:Chromatography, Affinity; D000242:Cyclic AMP / Q000737:chemistry; D015180:Electrophoresis, Gel, Two-Dimensional; D008274:Magnesium / Q000378:metabolism; D008297:Male; D008970:Molecular Weight; D010750:Phosphoproteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D010766:Phosphorylation; D012474:Salmon; D013081:Sperm Motility; D013082:Sperm Tail / Q000502:physiology*; D013737:Testis / Q000737:chemistry*
D010750:Phosphoproteins; D000242:Cyclic AMP; D008274:Magnesium; D002118:Calcium