Purification and preliminary characterization of phosphoglycerate mutase from Schizosaccharomyces pombe.
Phosphoglycerate mutase could be purified to over 95% homogeneity by a single step procedure involving elution from Cibacron Blue-Sepharose by a pulse of cofactor 2,3-bisphosphoglycerate. Although the enzyme has been isolated in only small quantities (c. 100 micrograms), gel filtration and sodium dodecylsulphate polyacrylamide gel electrophoresis indicated that it is monomeric with Mr approximately 23,000, an extremely low value for this enzyme. Preliminary investigations of the kinetic characteristics and the nature of important amino acid side chains have been undertaken.
D003931:Diacetyl / Q000494:pharmacology; D004047:Diethyl Pyrocarbonate / Q000494:pharmacology; D007700:Kinetics; D008970:Molecular Weight; D010736:Phosphoglycerate Mutase / Q000302:isolation & purification* / Q000378:metabolism; D010770:Phosphotransferases / Q000302:isolation & purification*; D004718:Saccharomycetales / Q000201:enzymology*; D012568:Schizosaccharomyces / Q000201:enzymology*; D013776:Tetrathionic Acid / Q000494:pharmacology; D014639:Vanadium / Q000494:pharmacology
D014639:Vanadium; D013776:Tetrathionic Acid; D010770:Phosphotransferases; D010736:Phosphoglycerate Mutase; D003931:Diacetyl; D004047:Diethyl Pyrocarbonate