Chanoine C, Saadi A, Guyot-Lenfant M, Hebbrecht C, Gallien C L
Laboratoire de Biologie du Développement, UA CNRS 1188, Université René Descartes, Paris, France.
FEBS Lett. 1990 Dec 17;277(1-2):200-4. doi: 10.1016/0014-5793(90)80844-9.
Myosin extracts from central white fibers and peripheral red fibers of the lateral muscle of eel (Anguilla anguilla) were analysed by electrophoresis under non-dissociating conditions, which demonstrated a polymorphism of myosin isoforms. The light and heavy subunit content of the isomyosins was established using SDS-PAGE and two-dimensional electrophoresis. In the central white muscle, 3 myosin isoforms FM3, FM2, FM1, were characterized by 3 types of fast light chain and one fast heavy chain HCf; the existence of a fourth isomyosin is discussed. In the peripheral red muscle, two myosin isoforms were found, SM1 and SM2, each characterized by a specific heavy chain, HCs1 or HCs2, and containing the same slow light chain content. This work demonstrates for the first time the existence of 3 heavy chains in the skeletal muscle of a fish.
对欧洲鳗鲡（Anguilla anguilla）侧肌中央白肌纤维和外周红肌纤维中的肌球蛋白提取物进行了非解离条件下的电泳分析，结果显示肌球蛋白同工型具有多态性。利用SDS-PAGE和二维电泳确定了同型肌球蛋白的轻链和重链含量。在中央白肌中，3种肌球蛋白同工型FM3、FM2、FM1，其特征为3种快速轻链和一种快速重链HCf；文中还讨论了第四种同型肌球蛋白的存在情况。在外周红肌中，发现了两种肌球蛋白同工型，SM1和SM2，每种同工型都有特定的重链，HCs1或HCs2，且慢链含量相同。这项工作首次证明了鱼类骨骼肌中存在3种重链。
