从软体动物平滑肌中分离和鉴定钙调蛋白。

Isolation and characterization of calmodulin from a molluscan smooth muscle.

作者信息

Mimura T, Yamanobe T, Sugi H

出版信息

Comp Biochem Physiol B. 1985;81(3):559-63. doi: 10.1016/0305-0491(85)90366-9.

Abstract

Calmodulin was purified from the anterior byssal retractor muscle (ABRM) of a mollusc Mytilus edulis. Ca2+-induced conformational changes in the ABRM calmodulin could be demonstrated by polyacrylamide gel electrophoresis, by u.v. absorption spectrum and by circular dichroic spectrum. The amino acid composition of the ABRM calmodulin closely resembled that of other invertebrate calmodulins. The ABRM calmodulin was less effective in activating rat brain phosphodiesterase than vertebrate calmodulins.

摘要

钙调蛋白是从贻贝的前足丝牵缩肌（ABRM）中纯化得到的。通过聚丙烯酰胺凝胶电泳、紫外吸收光谱和圆二色光谱可以证明钙离子诱导的ABRM钙调蛋白的构象变化。ABRM钙调蛋白的氨基酸组成与其他无脊椎动物钙调蛋白非常相似。ABRM钙调蛋白在激活大鼠脑磷酸二酯酶方面比脊椎动物钙调蛋白的效果要差。