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Polymorphism of myofibrillar proteins in histochemically identified myotomal muscle fibre types of Heteropneustes fossilis (Bloch) and Labeo rohita (Hamilton)
Author(s) -
Jasra P. K.,
Talesara C. L.,
Kiran Shashi
Publication year - 1991
Publication title -
journal of fish biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.672
H-Index - 115
eISSN - 1095-8649
pISSN - 0022-1112
DOI - 10.1111/j.1095-8649.1991.tb03103.x
Subject(s) - labeo , heteropneustes fossilis , myofibril , biology , myosin , myh7 , skeletal muscle , anatomy , medicine , endocrinology , biochemistry , myosin light chain kinase , fish <actinopterygii> , fishery , catfish
Myofibrillar proteins in the myotomal muscle fibre types of two freshwater teleosts, Heteropneustes fossilis (Bloch) and Labeo rohita (Hamilton), were investigated. The fibre types were identified histochemically based on the reactivities of the enzymes SDH and m ‐ATPase. Electrophoretic analysis revealed distribution patterns of myosin light chains, tropomyosin, troponin, c ‐ and m ‐protein; specific to the muscle fibre types. The results correlate well with the general pattern of myofibrillar protein distribution found in the skeletal muscles of higher vertebrates. The significance of the present findings are discussed with regard to histochemical, biochemical as well as functional properties of the muscle fibre types.