Abstract

Functional and structural properties of L-lactate dehydrogenase (LDH, EC 1.1.1.27) from embryos of various fish species (Atlantic salmon, rainbow trout, autumn cisco, least [Siberian] cisco, Siberian sturgeon, sterlet, loach, carp, goldfish, and zebrafish) were analysed. The minimum Km for pyruvate from embryos is correlated with the optimal temperatures of development in nature. LDH from embryos of fish adapted to low environmental temperatures (salmon and rainbow trout) shows lower Arrhenius activation energy and thermal stability values, than those from embryos of other fish species.

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