Abstract
The electrophoretic mobility, substrate stereospecificity, and apparent Michaelis constant ( K m ) values for lactic acid, pyruvic acid, and nicotinamide adenine dinucleotide (oxidized and reduced forms) were examined for the lactic dehydrogenase (LDH) of cell-free extracts of normal mouse erythrocytes and host cell-free P. berghei. The parasite enzyme was electrophoretically distinct from the LDH of the host cell. Both LDH's were stereospecific for l(+) lactic acid. No significant differences existed between the host cell and the parasitic LDH's in the K m values for lactic acid and nicotinamide adenine dinucleotide (oxidized and reduced forms). However, the value for pyruvate with the parasite LDH was 1 36 th that of the host cell enzyme showing an increased affinity of the former system for pyruvate. The parasitic LDH had higher specific acitivities with both lactic acid and pyruvic acid than did the host cell enzyme.
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