title: Purification and properties of the phosphoglycerate mutase isozymes from the mouse.
abstract: The two homodimeric isozymes of phosphoglycerate mutase have been purified from murine kidney and muscle. No differences were observed in the Michaelis-Menten constant for the substrate 2-phospho-D-glycerate, in molecular weight, temperature and pH optima, when the purified isozymes were compared. The isozymes differ in their inhibition constants for phosphoenolpyruvate, in their Michaelis constants for 3-phospho-D-glycerate and 2,3-bisphospho-D-glycerate, their thermal and pH lability and in their sensitivity towards mercury ions.
mesh_terms: D000818:Animals; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D051379:Mice; D009132:Muscles / Q000201:enzymology; D010736:Phosphoglycerate Mutase / Q000302:isolation & purification* / Q000378:metabolism; D010770:Phosphotransferases / Q000302:isolation & purification*; D014018:Tissue Distribution
chemical_list: D007527:Isoenzymes; D010770:Phosphotransferases; D010736:Phosphoglycerate Mutase