Purification of 2,3-bisphosphoglycerate synthase-phosphatase from pig skeletal muscle.
Two enzymes which possess 2,3-bisphosphoglycerate synthase, 2,3-bisphosphoglycerate phosphatase and phosphoglycerate mutase activities have been purified from pig skeletal muscle. One of the enzymes corresponds to type M phosphoglycerate mutase. The other enzyme shows properties similar to those of the 2,3-bisphosphoglycerate synthase-phosphatase present in mammalian erythrocytes. The erythrocyte and the muscle enzyme possess the same molecular (56 000) and subunit (27 000) weights. The synthase, phosphatase and mutase activity ratio is similar in both enzymes, and they are affected by the same inhibitor (glycerate 3-P) and activators (glycolate 2-P, pyrophosphate, sulfite and bisulfite).
D000818:Animals; D004789:Enzyme Activation; D005988:Glyceric Acids / Q000494:pharmacology; D046911:Macromolecular Substances; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology; D010733:Phosphoglucomutase / Q000302:isolation & purification*; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification*; D013447:Sulfites / Q000494:pharmacology; D013552:Swine; D013776:Tetrathionic Acid / Q000494:pharmacology
D005988:Glyceric Acids; D046911:Macromolecular Substances; D013447:Sulfites; C019794:bisphosphoglycerate phosphatase; C005156:3-phosphoglycerate; D013776:Tetrathionic Acid; D010744:Phosphoric Monoester Hydrolases; D010733:Phosphoglucomutase