Sobota A, Cusinato F, Luciani S
Department of Pharmacology, University of Padova, Italy.
Biochem Biophys Res Commun. 1990 Nov 15;172(3):1067-72. doi: 10.1016/0006-291x(90)91555-7.
Calpactins were purified from bovine cardiac muscle by a slightly modified Glenney et al. procedure (J. Cell. Biol. 104, 503-511, 1987). Two major proteins (apparent MW of 36 and 68 kDa) able to bind phospholipids in a Ca2(+)-dependent manner were identified. These proteins completely reversed the inhibition of Na+/Ca2+ exchange activity of cardiac sarcolemmal vesicles consequent to EGTA-treatment. A modulation of cardiac Na+/Ca2+ exchange activity by calpactins is suggested.
通过对Glenney等人的方法（《细胞生物学杂志》104卷，503 - 511页，1987年）进行轻微修改，从牛心肌中纯化出了钙结合蛋白。鉴定出了两种主要蛋白质（表观分子量分别为36 kDa和68 kDa），它们能够以Ca2+依赖的方式结合磷脂。这些蛋白质完全逆转了因EGTA处理导致的心肌肌膜囊泡Na+/Ca2+交换活性的抑制。提示钙结合蛋白对心肌Na+/Ca2+交换活性有调节作用。
