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Polymorphism of white muscle myosin and parvalbumins in the genus Barbus (Teleostei: Cyprinidae)
Author(s) -
Huriaux F.,
Vandewalle P.,
Focant B.
Publication year - 1992
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.1095-8649.1992.tb02716.x
Subject(s) - barbel , biology , barbus , cyprinidae , teleostei , zoology , subfamily , myosin , white (mutation) , anatomy , genetics , fishery , gene , biochemistry , fish <actinopterygii>
Muscle proteins were investigated in two large European barbels, Barbus barbus and B. meridionalis , and in four small tropical barbels native to SE Asia: B. conchonius , B. tetrazona , B. sachsi and B. titteya . Polyacrylamide gel electrophoresis was used to analyse myosin heavy and light chains and parvalbumin isotypes from white trunk muscle. Each species could be biochemically identified. The myosin subunit and parvalbumin isotype patterns obtained for the two European barbels were similar. The Asian barbels, on the other hand, not only differed from the European species but displayed a greater diversity within their group. These biochemical results are largely in agreement with morphological and genetic data, but fail to substantiate suggested close relationships between Asian barbel species.