LaFramboise W A, Daood M J, Guthrie R D, Moretti P, Schiaffino S, Ontell M
Department of Neurobiology, University of Pittsburgh School of Medicine, PA 15261.
Biochim Biophys Acta. 1990 Jul 20;1035(1):109-12. doi: 10.1016/0304-4165(90)90181-u.
One slow and three fast myosin heavy chains have been described in typical skeletal muscles of the adult rat using immunocytochemical analysis. Electrophoretic isolation and immunochemical identification of these four isoforms has not been achieved. An electrophoretic procedure is described which, by altering the cross-linkage and polymerization kinetics of 5% polyacrylamide gels, allows resolution of these four distinct myosin heavy chains. Using specific monoclonal antibodies and double immunoblotting analysis, the identity and electrophoretic migration order of the myosin heavy chains was established to be: 2A less than 2X less than 2B less than beta/slow.
通过免疫细胞化学分析，在成年大鼠的典型骨骼肌中已发现一条慢速和三条快速肌球蛋白重链。尚未实现这四种异构体的电泳分离和免疫化学鉴定。本文描述了一种电泳方法，通过改变5%聚丙烯酰胺凝胶的交联和聚合动力学，可分离这四种不同的肌球蛋白重链。使用特异性单克隆抗体和双重免疫印迹分析，确定了肌球蛋白重链的身份和电泳迁移顺序为：2A < 2X < 2B < β/慢速。
