Kodentsova V M, Sokol'nikov A A, Vrzhesinskaia O A, Spirichem V B
Biokhimiia. 1991 Apr;56(4):727-32.
It was found that the activity of spectrin-dependent ATPase of erythrocyte ghosts isolated from rats with alimentary deficiency of vitamin K was significantly increased as compared with control animals, whereas in rats kept on a vicasol-rich diet this parameter was unchanged. In vitamin K-deficient rats the amount of proteins loosely bound to erythrocyte membranes was significantly reduced. At the same time, the activity of the integral enzyme (Na, K-ATPase) did not depend on the vitamin K provision despite the fact that in vitamin K-deficient animals kept on a vicasol-rich diet the enzyme affinity for ouabain was strongly decreased as compared with control. It was suggested that this effect might be due to the changes in the lipid and protein environment of the membrane-bound enzyme. Administration of the antivitamin K, pelentane, did not induce any conspicuous changes in the enzyme activities. It was concluded that antivitamin K does not induce any modification of the properties of erythrocyte-linked enzymes observed under conditions of vitamin K deficiency.
研究发现，与对照动物相比，从维生素K膳食缺乏的大鼠分离出的红细胞膜血影蛋白依赖性ATP酶活性显著增加，而在富含维生素K的饮食喂养的大鼠中，该参数未发生变化。在维生素K缺乏的大鼠中，松散结合于红细胞膜的蛋白质数量显著减少。同时，尽管在富含维生素K的饮食喂养的维生素K缺乏动物中，该酶对哇巴因的亲和力与对照相比大幅降低，但完整酶（钠钾ATP酶）的活性并不依赖于维生素K的供应。有人认为，这种效应可能是由于膜结合酶的脂质和蛋白质环境发生了变化。给予抗维生素K（培拉汀）并未引起酶活性的任何明显变化。得出的结论是，抗维生素K不会诱导在维生素K缺乏条件下观察到的红细胞相关酶特性的任何改变。
