Abstract
Lactate dehydrogenase ( l-lactate:NAD oxidoreductase, EC 1.1.1.27) from embryonic chick liver had different kinetic and thermal stability properties from lactate dehydrogenase from adult chick liver, and lactate dehydrogenase prepared from different sources known to contain varying percentages of the lactate dehydrogenases 1, 2, 3, 4 and 5 isozymes. The embryonic chick liver lactate dehydrogenase could not be separated from adult chick liver lactate dehydrogenases or lactate dehydrogenase 5 on the basis of its electrophoretic mobility on polyacrylamide disc gels. However, embryonic chick liver lactate dehydrogenase utilized α-ketoglutaric acid as a substrate, and 3-acetylpyridine NAD as a coenzyme more efficiently than any of the other lactate dehydrogenase isozymes. Also embryonic chick liver lactate dehydrogenase was more resistant to heating at 65°C than the other lactate dehydrogenase isozymes. Further experiments showed that the kinetic properties of embryonic chick liver lactate dehydrogenase were consistent with those demonstrated for lactate dehydrogenase X.
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