牛心线粒体基质中热稳定钙调蛋白结合蛋白的纯化与鉴定
Purification and characterization of the heat-stable calmodulin-binding protein from the matrix of bovine heart mitochondria.
作者信息
Hatase O, Tokuda M, Sharma R K, Wang J H, Green D E
出版信息
Biochem Biophys Res Commun. 1983 Jun 15;113(2):633-7. doi: 10.1016/0006-291x(83)91773-4.
PMID:6870876
Abstract
A heat-stable calmodulin binding protein was purified and characterized from the matrix of bovine heart mitochondria. It bound specifically to calmodulin in the presence of calcium, and strongly inhibited the stimulatory activity of calmodulin on phosphodiesterase. The estimated molecular weight of the calmodulin-binding protein was 61,000 dalton determined by SDS-polyacrylamide gel electrophoresis.
摘要
从牛心脏线粒体基质中纯化并鉴定出一种热稳定的钙调蛋白结合蛋白。在有钙存在的情况下，它能特异性地与钙调蛋白结合，并强烈抑制钙调蛋白对磷酸二酯酶的刺激活性。通过SDS-聚丙烯酰胺凝胶电泳测定，钙调蛋白结合蛋白的估计分子量为61,000道尔顿。
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