Abstract
Summary
Spectrophotometric analysis of chick lactate dehydrogenase activity showed that the LDH in breast muscle supernatant and isolated LDH 5 had greater activity at high pyruvate concentration than at low. The difference was more marked at 40°C than at lower temperatures. Heart muscle LDH, and isolated LDH 1 reacted best at low pyruvate concentration. The difference was less marked at 40°C than at lower temperatures.
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