Nakamura M, Michikawa Y, Baba T, Okinaga S, Arai K
Department of Obstetrics and Gynecology, School of Medicine, Teikyo University, Tokyo, Japan.
Biochem Biophys Res Commun. 1992 Jul 31;186(2):668-73. doi: 10.1016/0006-291x(92)90798-p.
We have already succeeded in purifying a calcium-binding protein (CalBP) from rat spermatogenic cells [Nakamura et al., Biochem. Biophys. Res. Commun., 176 (1991) 1358]. In this study, the location of this protein within rat testis was examined, using a rabbit antisera for this protein. The antigen was localized on the developing acrosomes during spermiogenesis. The NH2-terminal amino acid sequence obtained for rat CalBP was identical to that of calreticulin obtained for the skeletal muscle of mice and closely resembled that for rabbit calreticulin. On the immunoblot analysis, the purified rat CalBP reacted with an antibody raised against rabbit skeletal muscle calreticulin. The results indicate that calreticulin is present in the acrosome of spermatids of rat testes.
我们已经成功地从大鼠生精细胞中纯化出一种钙结合蛋白（CalBP）[中村等人，《生物化学与生物物理研究通讯》，176 (1991) 1358]。在本研究中，使用针对该蛋白的兔抗血清检测了该蛋白在大鼠睾丸中的定位。抗原定位于精子发生过程中正在发育的顶体上。大鼠CalBP的氨基末端氨基酸序列与从小鼠骨骼肌中获得的钙网蛋白的序列相同，并且与兔钙网蛋白的序列非常相似。在免疫印迹分析中，纯化的大鼠CalBP与针对兔骨骼肌钙网蛋白产生的抗体发生反应。结果表明，钙网蛋白存在于大鼠睾丸精子细胞的顶体中。
