Myosin structure in the eel ( Anguilla anguilla L)

• Published in: FEBS Letters
• Main Authors: Chanoine, C., Saadi, A., Guyot-Lenfant, M., Hebbrecht, C., Gallien, Cl.L.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 1990
• Subjects: Cell Biology; Genetics; Molecular Biology; Biochemistry; Structural Biology; Biophysics; Anguilla anguilla
• Online Access: http://dx.doi.org/10.1016/0014-5793(90)80844-9; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793%2890%2980844-9; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793(90)80844-9; https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2890%2980844-9

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 eleetrophoresis. In the central white muscle, 3 myosin isoforms FM3, FM2, FMI, 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.