Abstract
1. 1.|The kinetic behaviour of lactate dehydrogenases (LDH's) from skeletal muscle from the extremities and deep parts of the body of the chamois ( Rupicapra rupicapra L.) was examined over a wide range of temperatures. 2. 2.|One species of LDH is observed in the heterothermic leg muscle and two in the homeothermic tissue. 3. 3.|When pH of the assay medium is “corrected” for temperature to conform to temperature-caused changes observed in the pH of intra and extracellular fluids, the homeothermic and heterothermic LDH's may be differentiated kinetically. 4. 4.|Strikingly, under such conditions a decrease in temperature does not bring about an increase in apparent affinity of the heterothermic LDH for substrate. Rather, values of the apparent Km for pyruvate remain constant, with the result that the Q 10 of the reaction remains unchanged over the entire range of temperature and substrate concentrations tested. 5. 5.|The significance of this behaviour under conditions that we believe approach the physiological one is discussed.
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