PMID: 10303Nov 10, 1976

Isolation and partial characterization of monophosphoglycerate mutase from human erythrocytes.

The Journal of Biological Chemistry
R H Sheibley, L F Hass

Abstract

Monophosphoglycerate mutase has been purified to homogeneity from outdated human erythrocytes as indicated by exclusion chromatography, polyacrylamide gel electrophoresis, and equilibrium centrifugation. Occasionally, the recommended purification procedure yields a small amount (3% or less) of a single extraneous protein which can be deleted from the enzyme preparation by employing an additional purification step. The native enzyme has a molecular weight of 54,000 to 56,000 as determined by equilibrium centrifugation and exclusion chromatography. Disc gel electrophoresis in the presence of sodium dodecyl sulfate yields a single protein band with a molecular weight of 28,600, indicating that the native macromolecule is a dimer composed of subunits of similar mass. Homogeneous monophosphoglycerate mutase is free of diphosphoglycerate mutase, enolase, and nonspecific phosphatase activities; however, the enzyme manifests intrinsic 2,3-diphospho-D-glycerate phosphatase activity as shown by thermal denaturation studies. The diphosphatase activity is stimulated by PPi and glycolate-2-P, but is inhibited by Cl-, HSO3-, and Pi. The pH optimum for both the diphosphatase and the mutase is 6.8. The Km for 2,3-diphospho-D-glycerate in the p...Continue Reading

Related Concepts

Amino Acids
Diphosphoglyceric Acids
Erythrocytes
Homo sapiens
Hydrogen-Ion Concentration
Kinetics
Molecular Weight
Phosphoglycerate Mutase
Phosphoric Monoester Hydrolases
Phosphotransferases

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