Comparative electrophoretic studies on the tissue proteins of some cat fishes

A.U. Hasnain, A.Q. Siddiqui


A comparative study on the soluble eye lens proteins, muscle myogens and multiple haemoglobins of four cat fishes has been made using starch gel electrophoresis. The whole eye lens protein patterns in air-breathing fish species remain consistent, while those of non-air-breathing species showed minor variations towards the cathode. However, white and red muscle as well as multiple haemoglobin electropherograms were devoid of individual differences in all the species. In the acid format gels, globins of Heteropneustes fossilis did not resolve into constituent polypeptide chains, but three obtained in urea starch medium. Two of them had electrophoretic mobilities equal to the chains of Clarias batrachus, which were resolved into the same number of chains in both the media. Haemoglobins of air-breathing species were resolved into the same number of multiple forms over a pH range of 6.8 to 8.5; but those of non air-breathing fishes moved in aggregated form at pH lower than 7.0. It is suggested that this property may be advantageous to air-breathing species which have to withstand drought conditions


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