A major calmodulin-binding protein common to various vertebrate tissues.
A major calmodulin-binding protein common to various vertebrate tissues.
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一种主要的钙调蛋白结合蛋白，常见于各种脊椎动物组织。
DOI：
10.1073/pnas.79.12.3780
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发表时间：
1982
影响因子：
11.1
通讯作者：
Greengard,P
中科院分区：
文献类型：
--
作者：
Palfrey,HC;Schiebler,W;Greengard,P
一个主要的钙调素结合蛋白（CaM-BP）的Mr 240，000证明在各种大鼠组织中使用125 I标记的钙调素凝胶覆盖技术。该蛋白质（命名为p240）中检测到的颗粒部分，并在较小程度上在所有研究组织的胞质溶胶。CaM与p240的结合完全依赖于Ca ~（2+）。第二，专门可溶性，CaM-BP（Mr 115，000）常见的几种组织和一些其他的CaM-BP与更有限的组织分布，也观察到通过使用这种技术。钙调素结合p240发生在大量的质膜从鸟类红细胞，但没有从哺乳动物红细胞膜。抗火鸡红细胞p240的抗体（抗TP 240）与其他组织中的p240交叉反应。通过证明125 I标记的钙调素可以结合p240特异性免疫沉淀从大鼠脑或火鸡红细胞的抗TP 240和钙调素之间的蛋白质识别的身份得到证实。p240可能与先前描述的肌动蛋白结合蛋白有关，并且可能代表CaM在细胞骨架上的主要作用位点。
A major calmodulin-binding protein (CaM-BP) of Mr 240,000 was demonstrated in various rat tissues by using a 125I-labeled CaM gel overlay technique. This protein (designated p240) was detected in the particulate fraction and to a lesser extent in the cytosol of all tissues studied. Binding of CaM to p240 was completely dependent on Ca2+. A second, exclusively soluble, CaM-BP (Mr115,000) common to several tissues and a number of other CaM-BPs with a more restricted tissue distribution were also observed by using this technique. CaM binding to p240 occurred in high amounts in plasma membranes from avian erythrocytes but was absent from mammalian erythrocyte membranes. Antibodies prepared against turkey erythrocyte p240 (anti-Tp240) crossreacted with p240 in other tissues. Identity between the proteins recognized by anti-Tp240 and CaM was confirmed by demonstrating that 125I-labeled CaM could bind to p240 specifically immunoprecipitated from either rat brain or turkey erythrocytes by anti-Tp240. The p240 may be related to a previously described actin-binding protein and may represent a major site of action of CaM on the cytoskeleton.