Human erythrocyte phosphoglycerate mutase: Evidence for normal catalysis in the absence of added 2,3-bisphospho-D-glycerate

This publication has 21 references indexed in Scilit:

• Phosphoglycerate mutases: stereochemical course of the phosphoryl group transfers catalyzed by the cofactor-dependent enzyme from rabbit muscle and the cofactor-independent enzyme from wheat germ
  Biochemistry, 1980
• Red cell phosphoglycerate mutase and bisphosphoglycerate synthase: Controlled modifications in coulombic properties in vitro
  Biochemical and Biophysical Research Communications, 1978
• Immunochemical and Enzymatic Properties of Bisphosphoglyceromutase/phosphatase and Phosphoglyceromutase from Human Erythrocytes
  European Journal of Biochemistry, 1978
• Phosphoglycerate mutase from wheat germ: studies with isotopically labeled 3-phospho-D-glycerates showing that the catalyzed reaction is intramolecular. Appendix: Phosphoglycerate mutase from wheat germ: isolation, crystallization, and properties
  Biochemistry, 1977
• Phosphoglycerate mutase from wheat germ: studies with oxygen-18-labeled substrate, investigations of the phosphatase and phosphoryl transfer activities, and evidence for a phosphoryl-enzyme intermediate
  Biochemistry, 1977
• The phosphorylation of yeast phosphoglycerate mutase
  Archives of Biochemistry and Biophysics, 1971
• Evidence for a phosphohistidine protein intermediate in the phosphoglycerate mutase reaction
  Archives of Biochemistry and Biophysics, 1970
• The 2,3-diphosphoglyceric acid phosphatase activity of phosphoglyceric acid mutase purified from human erythrocytes
  Archives of Biochemistry and Biophysics, 1970
• Influence of salt, substrate, and cofactor concentrations on the kinetic and mechanistic behavior of phosphoglycerate mutase
  Biochemistry, 1968
• [26] Phosphoglyceric Acid Mutase
  Published by Elsevier ,1962