D. Harkness, S. Roth
Mar 31, 1969
Citations
1
Influential Citations
31
Citations
Journal
Biochemical and biophysical research communications
Abstract
Abstract A 1200-fold purification of an enzyme from human erythrocytes which hydrolyzes 2,3-diphosphoglyceric acid (2, 3-DPG) to Pi and 3-phosphoglyceric acid (3-PGA) is described. The preparation is free of acid phosphatase and phosphoglycerate mutase. Enzyme activity is enhanced 37-fold by 20mM bisulfite. Dithionite and cyanide also cause stimulation. The pH optimum is 7.5 and the K m for 2,3-DPG is 4×10 −5 M. Enzyme activity is inhibited by both 3-PGA and 2-PGA. It is believed that this enzyme, and not PGA mutase which in the presence of inorganic pyrophosphate has this same phosphatase activity, is the physiological intracellular phosphatase for 2,3-DPG in erythrocytes.