Abstract
Soluble proteins of skeletal muscles of four species of genus Channa have been analyzed by native and SDS-containing polyacryalmide gel electrophoresis (SDS-PAGE). Native-PAGE patterns of soluble skeletal muscle proteins of all four species are devoid of intraspecies qualitative variations. Sixteen protein bands, each with characteristic electrophoretic mobility, are diagnostic to Channa gachua and C. striatus, while 10 and 15 bands are to C. marulius and C. punctatus, respectively. In the same sequence of species, the total number of representative polypeptides in SDS-PAGE patterns is: 18, 14, 13 and 21, respectively. Among species-marker bands, highly acidic proteins are most prominent. Species specific polypeptides have also been identified after resolving soluble muscle proteins by SDS-PAGE. Intraspecies quantitative differences within the individual bands exist in native as well as SDS-PAGE systems; but, contrary to native electrophoretic system, SDS-PAGE patterns of the soluble muscle proteins display a certain degree of numerical heterogeneity also. Most obvious differences are observed in polypeptides with in the Mr range of 26-44 kD, which could be placed under variability-groups of consistency. Identified species-marker bands resolved in either of the electrophoretic systems can also be used for identifying the hybrids and settling taxonomic controversies. In order to facilitate the use of data by other workers, the molecular weights of each band in SDS-PAGE and the relative electrophoretic mobilities of species marker patterns in native gels have been documented.
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