Protein kinase activity in commercially available crystalline yeast alcohol dehydrogenase.
Commercially available crystalline yeast alcohol dehydrogenase contained protein kinase activity. Casein and phosvitin were readily phosphorylated, but whole calf thymus histone was not. The protein kinase activity was inhibited by KCl, was not stimulated by cyclic AMP and could be separated from the alcohol dehydrogenase activity by sucrose density centrifugation.
D000429:Alcohol Oxidoreductases / Q000032:analysis*; D000818:Animals; D002364:Caseins; D002417:Cattle; D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D000242:Cyclic AMP; D004527:Egg Proteins; D005069:Evaluation Studies as Topic; D006657:Histones; D010750:Phosphoproteins; D010759:Phosphorus Isotopes; D010770:Phosphotransferases / Q000032:analysis*; D011189:Potassium Chloride; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013056:Spectrophotometry, Ultraviolet; D013950:Thymus Gland
D002364:Caseins; D004527:Egg Proteins; D006657:Histones; D010750:Phosphoproteins; D010759:Phosphorus Isotopes; D047428:Protein Kinase Inhibitors; D011189:Potassium Chloride; D000242:Cyclic AMP; D000429:Alcohol Oxidoreductases; D010770:Phosphotransferases; D011494:Protein Kinases