Sheaves R M, Bowman D, Hope D B
J Neurochem. 1982 Oct;39(4):909-14. doi: 10.1111/j.1471-4159.1982.tb11476.x.
Calmodulin was isolated as an electrophoretically homogeneous protein from bovine posterior pituitary glands. The yield indicated that this gland is a particularly rich source. Purified bovine posterior pituitary calmodulin and bovine brain calmodulin had identical electrophoretic mobilities on 10% and 12% polyacrylamide gels. The protein was further identified by molecular weight determination and by amino acid analysis which showed that it contained trimethyllysine, one residue per molecule. Bovine posterior pituitary calmodulin was found to activate a preparation of calmodulin-deficient phosphodiesterase from bovine heart. In addition, pituitary calmodulin stimulated Ca+ + Mg2+-ATPase activity associated with a purified nerve ending plasma membrane fraction. This dependence could only be demonstrated after successive washing of the membranes with EGTA buffers, a procedure designed to remove endogenous calmodulin.
钙调蛋白是从牛脑垂体后叶中分离出来的一种电泳纯蛋白质。产量表明该腺体是一个特别丰富的来源。纯化的牛脑垂体后叶钙调蛋白和牛脑钙调蛋白在10%和12%的聚丙烯酰胺凝胶上具有相同的电泳迁移率。通过分子量测定和氨基酸分析进一步鉴定了该蛋白质，结果表明它含有三甲基赖氨酸，每个分子一个残基。发现牛脑垂体后叶钙调蛋白可激活来自牛心脏的钙调蛋白缺陷型磷酸二酯酶制剂。此外，垂体钙调蛋白刺激了与纯化的神经末梢质膜部分相关的Ca²⁺-Mg²⁺-ATP酶活性。只有在用EGTA缓冲液连续洗涤膜后才能证明这种依赖性，该程序旨在去除内源性钙调蛋白。
