Lactate Dehydrogenase Isozymes: Substrate Inhibition in Various Human Tissues

Abstract

The total lactate dehydrogenase (LDH) in whole homogenates of various human tissues reacts more similarly toward pyruvate and lactate at 25 degrees C than expected from the marked differences in substrate inhibition at this temperature between isolated, purified LDH-1, and LDH-5. At 37 degrees C, LDH-5 closely resembles LDH-1 in extent of inhibition by substrate. These results are incompatible with the theory that differences in degree of isozyme inhibition by substrate have resulted in predominance of LDH-5 in aerobic tissues and predominance of LDH-1 in aerobic tissues.