Fujinoki Masakatsu, Kawamura Takeshi, Toda Toshifusa, Ishimoda-Takagi Tadashi, Ohtake Hideki, Shimizu Nobuyoshi, Okuno Makoto
Department of Physiology, Dokkyo University School of Medicine, Mibu, Tochigi.
Department of Molecular Biology, Keio University School of Medicine, Shinanomachi, Shinjuku-ku, Tokyo.
Reprod Med Biol. 2004 Aug 10;3(3):133-139. doi: 10.1111/j.1447-0578.2004.00061.x. eCollection 2004 Sep.
Sperm motility is regulated by protein phosphorylation. The 66 kDa protein obtained from hamster sperm flagella was phosphorylated at serine residues associated with the motility initiation. In order to understand the regulatory mechanism of sperm motility, the 66 kDa protein was identified in the present study. The 66 kDa protein was purified by 2-D gel electrophoresis and identified by matrix-assisted laser desorption ionization mass spectrometry, liquid chromatography-tandem mass spectrometry and peptide sequencer. The 66 kDa protein was tubulin β chain. The 66 kDa protein is one of the tubulin β chain isoforms and phosphorylated in relation to the motility initiation. (Reprod Med Biol 2004; : 133-139).
精子活力受蛋白质磷酸化调节。从仓鼠精子鞭毛中获得的66 kDa蛋白质在与活力起始相关的丝氨酸残基处发生磷酸化。为了解精子活力的调节机制,本研究对该66 kDa蛋白质进行了鉴定。通过二维凝胶电泳纯化该66 kDa蛋白质,并采用基质辅助激光解吸电离质谱、液相色谱-串联质谱和肽测序仪进行鉴定。该66 kDa蛋白质为微管蛋白β链。66 kDa蛋白质是微管蛋白β链同工型之一,与活力起始相关且发生了磷酸化。(《生殖医学与生物学》2004年;:133 - 139)