Iwata S, Shirasawa E, Takehana M
Curr Eye Res. 1984 May;3(5):717-21. doi: 10.3109/02713688409065593.
It has been hypothesized that an activator of Ca-ATPase co-exists with Ca-ATPase in the mouse lens. Though the Ca-ATPase activity could be measured from mouse lens homogenate, its activity could not be determined in individual soluble and insoluble fractions. The Ca-ATPase activity, however, could be detected when an activator of this enzyme such as calmodulin was added to the lens insoluble fraction. This enzyme in the lens insoluble fraction was activated also by addition of soluble fraction. The Ca-ATPase in homogenate was inhibited by chlorpromazine and N-(6-amino-hexyl)-5-chloro-1-naphthalenesulfonamide (W-7), which are calmodulin antagonists. When the mouse lens was incubated with W-7, the degree of the lens opacification increased in relation to W-7 concentration.
据推测，在小鼠晶状体中，钙 - ATP酶激活剂与钙 - ATP酶共存。虽然可以从小鼠晶状体匀浆中测量钙 - ATP酶活性，但无法在单个可溶性和不溶性组分中测定其活性。然而，当向晶状体不溶性组分中添加该酶的激活剂（如钙调蛋白）时，可以检测到钙 - ATP酶活性。通过添加可溶性组分，晶状体不溶性组分中的这种酶也被激活。匀浆中的钙 - ATP酶受到氯丙嗪和N -（6 - 氨基己基）-5 - 氯 - 1 - 萘磺酰胺（W - 7）的抑制，这两种物质都是钙调蛋白拮抗剂。当小鼠晶状体与W - 7一起孵育时，晶状体混浊程度随W - 7浓度的增加而增加。
