交联扇贝肌球蛋白的电子显微镜观察
Electron microscopy of cross-linked scallop myosin.
作者信息
Vibert P, Cohen C, Hardwicke P M, Szent-Györgyi A G
出版信息
J Mol Biol. 1985 May 25;183(2):283-6. doi: 10.1016/0022-2836(85)90221-9.
PMID:4009727
Abstract
The N-terminal regions of the regulatory light chains on the two heads of scallop myosin can be cross-linked to one another. Electron microscopy of cross-linked myosin molecules, and of dimers of myosin subfragment-1 produced by digesting them with papain, shows that the site of cross-linking is very close to the head-rod junction.
摘要
扇贝肌球蛋白两个头部上调节轻链的N端区域可以相互交联。对交联的肌球蛋白分子以及用木瓜蛋白酶消化产生的肌球蛋白亚片段-1二聚体进行电子显微镜观察，结果表明交联位点非常靠近头部-杆部连接处。
Zotero 插件