Fujinoki Masakatsu, Kawamura Takeshi, Toda Toshifusa, Ohtake Hideki, Ishimoda-Takagi Tadashi, Shimizu Nobuyoshi, Yamaoka Sadao, Okuno Makoto
Department of Physiology, Dokkyo University School of Medicine, 880 kitakobayasi, Mibu, Tochigi 321-0293, Japan.
Comp Biochem Physiol B Biochem Mol Biol. 2004 Apr;137(4):509-20. doi: 10.1016/j.cbpc.2004.02.006.
In our previous studies (Fujinoki et al., 2001, 2003), we reported that two types of 36 kDa proteins, designated 36K-A protein and 36K-B protein, obtained from hamster sperm flagella, are associated with motility activation and phosphorylated in a cAMP-dependent manner at serine residues. In the present experiments, we focused on the hamster (Mesocricetus auratus) 36K-A protein, which was analyzed by peptide mass finger printing and amino acid sequencing. The results suggest that 36K-A protein is a pyruvate dehydrogenase E1 component beta subunit lacking the N-terminal 30 amino acids. Moreover, our results suggest that 36 K-A protein is localized in the fibrous sheath of the principal piece of hamster spermatazoa.
在我们之前的研究中(藤木等人,2001年、2003年),我们报告称,从仓鼠精子鞭毛中获得的两种36 kDa蛋白,分别命名为36K - A蛋白和36K - B蛋白,与运动激活相关,并在丝氨酸残基处以cAMP依赖的方式发生磷酸化。在本实验中,我们聚焦于仓鼠(金黄仓鼠)的36K - A蛋白,通过肽质量指纹图谱和氨基酸测序对其进行了分析。结果表明,36K - A蛋白是一种丙酮酸脱氢酶E1组分β亚基,缺少N端的30个氨基酸。此外,我们的结果表明,36K - A蛋白定位于仓鼠精子主段的纤维鞘中。