Abstract
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.
MeSH Terms
Alcohol Oxidoreductases/analysis
Animals
Caseins
Cattle
Centrifugation, Density Gradient
Chromatography, Gel
Cyclic AMP
Egg Proteins
Evaluation Studies as Topic
Histones
Phosphoproteins
Phosphorus Isotopes
Phosphotransferases/analysis
Potassium Chloride
Protein Kinase Inhibitors
Protein Kinases/analysis,isolation & purification,metabolism
Saccharomyces cerevisiae/enzymology
Spectrophotometry, Ultraviolet
Thymus Gland
Chemicals
Caseins
Egg Proteins
Histones
Phosphoproteins
Phosphorus Isotopes
Protein Kinase Inhibitors
Potassium Chloride
Cyclic AMP
Alcohol Oxidoreductases
Phosphotransferases
Protein Kinases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kemp B E
Froscio M
Murray A W
References (11)
11 references, click to expand
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