On the mechanism of binding of calpastatin, the protein inhibitor of calpains, to biologic membranes.
On the mechanism of binding of calpastatin, the protein inhibitor of calpains, to biologic membranes.
复制标题
关于钙蛋白酶抑制剂钙蛋白酶抑制剂与生物膜结合的机制。
DOI：
10.1016/0006-291x(88)90501-3
复制
发表时间：
1988
影响因子：
3.1
通讯作者：
Mellgren,RL
中科院分区：
文献类型：
--
作者：
Mellgren,RL
牛心肌钙化蛋白是钙依赖蛋白水解酶的内源性抑制物，在中性pH和低离子强度的条件下，可以与肌浆网制剂结合。即使在100mMKCl2存在的情况下，每毫克膜也结合了4-5μg的钙调蛋白。虽然在牛心肌肌膜中发现了钙粘蛋白，但在分离的红细胞膜制剂中，犬和人的红细胞膜中都不存在钙粘蛋白。在低离子强度下，牛心肌钙调蛋白能与纯化的磷脂微囊结合，而人红细胞钙调蛋白则不能。因此，磷脂似乎参与了钙调蛋白与膜的结合。
Bovine myocardial calpastatin, the endogenous inhibitor of the calcium-dependent proteinases, calpains, could bind to sarcoplasmic reticulum preparations at neutral pH and low ionic strength. Even in the presence of 100 to 200 mM KCl, 4 to 5 μg of calpastatin was bound per mg of membrane. Although calpastatin is found associated with bovine myocardial sarcolemma, neither canine nor human erythrocyte calpastatins were present in isolated erythrocyte membrane preparations. The bovine myocardial calpastatin, but not human erythrocyte calpastatin, could associate with purified phospholipid vesicles at low ionic strength. Thus, phospholipids appear to be involved in the binding of calpastatin to membranes.