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Lactate dehydrogenase ec 1.1.1.27 isozymes in loach misgurnus fossilis development


, : Lactate dehydrogenase ec 1.1.1.27 isozymes in loach misgurnus fossilis development. Biokhimiya 43(3): 467-472

Isoenzyme patterns of lactate dehydrogenase (LDH, EC 1.1.1.27) were determined in the loach (M. fossilis) oocytes, unfertilized eggs, developing embryos and larvae, and sensitivity of the isoenzymes to the effect of AgNO3, p-chlormercurybenzoate and high temperature were investigated. The presence of 4 phenotypes of LDH patterns which differed in isozyme number, relative activity, electrophoretic mobility in polyacrylamide gel and in frequency of occurence in different populations of the investigated species was demonstrated. Before the hatching stage there appeared a new isozyme which was completely inhibited by AgNO3 and had the same electrophoretic mobility in all LDH phenotypes. During larvae development the content of this LDH isozyme increased. Some isozymes, especially those which had low anodic mobility and decreased in their relative quantity, disappeared during development of embryos and larvae. p-Chlormercurybenzoate in the concentration 1 mM and heating at 70.degree. C for 20 min did not significantly affect LDH activities in loach eggs, embryos and larvae.

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