The purification of yeast glucose 6-phosphate dehydrogenase by dye-ligand chromatography.
Glucose 6-phosphate dehydrogenase (EC 1.1.1.39) has been purified to homogeneity from baker's yeast by a simple procedure involving affinity elution from a column of red triazine dye, H-8BN, immobilized to Sepharose 6B. Eight milligrams of homogeneous protein is obtained in 53% yield from 200 g of dried yeast. This represents the first published purification of the enzyme from Saccharomyces Cerevisiae.
D002845:Chromatography / Q000379:methods; D004396:Coloring Agents; D005954:Glucosephosphate Dehydrogenase / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014227:Triazines
D004396:Coloring Agents; D014227:Triazines; C035666:Procion brilliant red H-8BN; D005954:Glucosephosphate Dehydrogenase