Kazennov A M, Rustamov F A, Frolova O V, Shalabodov A D
Zh Evol Biokhim Fiziol. 1996 Jul-Aug;32(4):393-401.
The removal of the membrane skeleton proteins (MSP), chiefly spectrin and actin, from the rat erythrocyte ghosts was shown to result in a decrease of both the total Na, K-ATPase activity and a partial reaction of the enzyme, namely the phosphatasic one. Besides, modulating effects of the effectors promoting the enzyme conformational transitions (ATP and Mg2+) on the ouabain-sensitive K-phosphatase is changed. For instance, a pronounced activation of the K-phosphate in a high-potassium medium in the presence of 1 mM ATP disappeared and the degree of the enzymatic activity enhancement in response to increasing MgCl2 concentrations (from 1.5 to 6 mM) is decreased. The data obtained are discussed from the viewpoint of possible involvement of the erythrocyte MSP in the catalytic of Na, K-ATPase.
从大鼠红细胞膜中去除膜骨架蛋白（MSP），主要是血影蛋白和肌动蛋白，结果显示钠钾ATP酶的总活性以及该酶的部分反应（即磷酸酶反应）均降低。此外，促进酶构象转变的效应物（ATP和Mg2+）对哇巴因敏感的钾磷酸酶的调节作用也发生了变化。例如，在1 mM ATP存在下，高钾培养基中钾磷酸酶的明显激活消失，并且随着MgCl2浓度从1.5 mM增加到6 mM，酶活性增强的程度降低。从红细胞MSP可能参与钠钾ATP酶催化作用的角度对所得数据进行了讨论。
