Abstract
The partial purification of phosphoglyceric acid mutase from human erythrocytes is described. This enzyme has an absolute requirement for 2,3-diphosphoglyceric acid under the conditions used for the assay. 2,3-Diphosphoglyceric acid phosphatase activity copurified with the mutase, and evidence that both of these activities are carried out by the same enzyme is reported. The phosphatase activity is markedly enhanced by inorganic pyrophosphate, 20- to 50-fold by 20 m m concentrations. In experiments utilizing 32P-labeled pyrophosphate, direct involvement in the reaction by pyrophosphate was excluded. Intracellular compounds in physiological concentrations failed to augment significantly the phosphatase activity of phosphoglyceric acid mutase. A second 2,3-diphosphoglyceric acid phosphatase which is stimulated by sodium bisulfite and unassociated with mutase activity was separated from the pyrophosphate-stimulated enzyme. The relative significance of these two enzymes in the metabolism of 2,3-diphosphoglyceric acid in the erythrocyte is discussed.
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