Acclimation temperature affects the functional and structural properties of lactate dehydrogenase from fish (Misgurnus fossilis) skeletal muscles

Abstract Acclimation of loach to low and high temperatures gives rise to certain changes in properties of M 4 -LDH from skeletal muscles. The apparent K m values for pyruvate of the enzyme purified from fish adapted to low temperatures shows a minimum at low measurement temperatures, whereas adaptation to high temperatures leads to the enzyme showing a minimum at high temperatures. The M 4 -LDH purified from fish acclimated to low temperatures reveals greater stability both to thermal and urea-induced inactivation. The differences in the kinetic properties of LDH from fish acclimated to low and high temperatures disappeared after treatment with urea and subsequent reactivation.