title: Myosin structure in the eel (Anguilla anguilla L.). Demonstration of three heavy chains in adult lateral muscle.
abstract: 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.
authors: Laboratoire de Biologie du Développement, UA CNRS 1188, Université René Descartes, Paris, France.
authors: C
authors: C
authors: Chanoine
authors: A
authors: A
authors: Saadi
authors: M
authors: M
authors: Guyot-Lenfant
authors: C
authors: C
authors: Hebbrecht
authors: C L
authors: CL
authors: Gallien
mesh_terms: D000818:Animals; D004524:Eels / Q000033:anatomy & histology*; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D015394:Molecular Structure; D009218:Myosins / Q000032:analysis / Q000648:ultrastructure*
chemical_list: D046911:Macromolecular Substances; D009218:Myosins