Abstract
Summary
Determinations of ATP-hexose phosphotransferase activity in chick embryo hearts demonstrated the presence of a soluble hexokinase. The enzyme has a low Km for glucose, a maximum activity at pH 8.0–8.5 and is inhibited by glucose-6-phosphate. Total enzyme activity does not change between the 5th and 7th day of development, decreases moderately thereafter and increases after hatching. The slight reduction of total enzyme activity observed between the 5th and 10th day of embryologic development is inadequate to account for the previously reported decrease in the maximal rate of intracellular glucose phosphorylation occurring in intact hearts during the same period.
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