Abstract
Rat islet homogenates display both phosphoglycerate 2,3-mutase and enolase activities. When phosphoglycerate 2,3-mutase is activated by 2,3-diphosphoglycerate, the reaction velocity becomes close to that of enolase. The islet content in 2,3-diphosphoglycerate is sufficiently high to allow virtually full activation of phosphoglycerate 2,3-mutase.
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