|Tropomyosin from the striated muscles of carp (Cyprinus carpio) and of icefish (Channichthys rhinoceratus)|Feller, G.; D'Haese, J.; Gerday, C. (1990). Tropomyosin from the striated muscles of carp (Cyprinus carpio) and of icefish (Channichthys rhinoceratus). Arch. Int. Phys. Bioch. 98(2): 297-305. dx.doi.org/10.3109/13813459009113990
In: Archives Internationales de Physiologie et de Biochimie. H. Vaillant-Carmanne: Liège. ISSN 0003-9799, more
|Authors|| || Top |
- Feller, G., more
- D'Haese, J.
- Gerday, C., more
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 α family and differ from higher vertebrate tropomyosin by the lack of β subunits. Specific α isotypes are however encountered in fast-twitch fibres (αw subunit) and slow-twitch or intermediate (pink) fibres (α and αw subunits). The amino acid compositions and the paracrystals formed by the carp aαwaαw and ααw tropomyosins do not differ markedly from that of rabbit αα chains. They differ however by their capability to inhibit the ATPase activity of rabbit skeletal muscle acto-HMM system. A β-like subunit is found in carp cardiac tropomyosin, in the proportion of 25% of the native protein, but not in icefish heart.