Inomata M, Imahori K, Kawashima S
Biochem Biophys Res Commun. 1986 Jul 31;138(2):638-43. doi: 10.1016/s0006-291x(86)80544-7.
Degradation of vimentin by native low calcium ion-requiring protease (mu CANP) was compared to that by autodigested mu CANP. On activation with 5 mM barium ions, a lag time was observed for the case of native mu CANP. This provides direct evidence that native mu CANP is inactive as a protease and must be autolyzed to be activated. Most of the protease activity can be accounted for by autodigested mu CANP with a 76 K polypeptide but another species with 50 K polypeptide may also be active.
将天然低钙需求蛋白酶(μ钙蛋白酶,mu CANP)对波形蛋白的降解作用与自身消化后的μ钙蛋白酶的降解作用进行了比较。在用5 mM钡离子激活时,观察到天然μ钙蛋白酶存在延迟期。这提供了直接证据,表明天然μ钙蛋白酶作为一种蛋白酶是无活性的,必须进行自身消化才能被激活。大部分蛋白酶活性可由具有76 K多肽的自身消化后的μ钙蛋白酶来解释,但另一种具有50 K多肽的类型也可能具有活性。