Tropomyosin from the Striated Muscles of Carp (Cyprinus Carpio) and of Icefish (Channichthys Rhinoceratus)

• Published in: Archives Internationales de Physiologie et de Biochimie
• Main Authors: Feller, Georges, D'Haese, J., Gerday, Charles
• Format: Article in Journal/Newspaper
• Language: English
• Published: Vaillant Carmanne 1990
• Subjects: Life sciences; Biochemistry; biophysics & molecular biology; Sciences du vivant; Biochimie; biophysique & biologie moléculaire; Icefish
• Online Access: https://orbi.uliege.be/handle/2268/16500; https://doi.org/10.3109/13813459009113990

peer reviewed Tropomyosin of fast-twitch, slow-twitch and cardiac muscles of carp and icefish has been isolated by hydroxyapatite chromatography. The subunit distribution has been investigated by polyacrylamide gel electrophoresis and by peptide mapping. The purified skeletal muscle tropomyosins all belong to the alpha family and differ from higher vertebrate tropomyosin by the lack of beta subunits. Specific alpha isotypes are however encountered in fast-twitch fibres (alpha w subunit) and slow-twitch or intermediate (pink) fibres (alpha and alpha w subunits). The amino acid compositions and the paracrystals formed by the carp alpha w alpha w and alpha alpha w tropomyosins do not differ markedly from that of rabbit alpha alpha chains. They differ however by their capability to inhibit the ATPase activity of rabbit skeletal muscle acto-HMM system. A beta-like subunit is found in carp cardiac tropomyosin, in the proportion of 25% of the native protein, but not in icefish heart.