Myosin structure in the eel (Anguilla anguilla L.). Demonstration of three heavy chains in adult lateral muscle.
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.
Chanoine
C
C
Laboratoire de Biologie du Développement, UA CNRS 1188, Université René Descartes, Paris, France.
Saadi
A
A
Guyot-Lenfant
M
M
Hebbrecht
C
C
Gallien
C L
CL
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*
D046911:Macromolecular Substances; D009218:Myosins