Distinction between cofactor-dependent and -independent phosphoglycerate mutases by chromatography on Cibacron Blue-Sepharose.
The binding of phosphoglycerate mutases from a variety of sources to Cibacron Blue-Sepharose has been examined. Those enzymes which are dependent on 2,3-bisphosphoglycerate (BPG) for activity bind to the immobilized dye and can be eluted by BPG. Those enzymes which are independent of BPG do not bind to the immobilized dye. The possible structural significance of this distinction is discussed.
D019794:2,3-Diphosphoglycerate; D000818:Animals; D001233:Aspergillus nidulans / Q000201:enzymology; D002175:Candida / Q000201:enzymology; D002417:Cattle; D002846:Chromatography, Affinity; D004396:Coloring Agents; D004163:Diphosphoglyceric Acids / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D004926:Escherichia coli / Q000201:enzymology; D009089:Mucor / Q000201:enzymology; D010736:Phosphoglycerate Mutase / Q000378:metabolism*; D010770:Phosphotransferases / Q000378:metabolism*; D010944:Plants / Q000201:enzymology; D011817:Rabbits; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012568:Schizosaccharomyces / Q000201:enzymology; D014227:Triazines / Q000378:metabolism*
D004396:Coloring Agents; D004163:Diphosphoglyceric Acids; D014227:Triazines; D019794:2,3-Diphosphoglycerate; C012842:Cibacron Blue F 3GA; D010770:Phosphotransferases; D010736:Phosphoglycerate Mutase