A cytoplasmic, cyclic nucleotide-independent casein kinase II from Saccharomyces cerevisiae
| Autor: | Eugeniusz Gasior, Kudlicki W, Ryszard Szyszka |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Cytoplasm
Macromolecular Substances Chemistry Protein subunit Biophysics Saccharomyces cerevisiae Biochemistry Molecular biology Phosphotransferase Structure-Activity Relationship Adenosine Triphosphate Structural Biology Casein Casein kinase 2 alpha 1 Guanosine Triphosphate Casein kinase 1 Casein kinase 2 Casein kinases Protein kinase A Casein Kinases Protein Kinases Molecular Biology |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 784:102-107 |
| ISSN: | 0167-4838 |
| DOI: | 10.1016/0167-4838(84)90115-8 |
| Popis: | Two molecular forms of casein kinase II (an ATP: protein phosphotransferase, EC 2.7.1.37) from yeast were isolated and characterized. The first form was composed of three polypeptide subunits with molecular weights of 41000, 37000 and 24000. The second form contained two larger polypeptides and lacked an autophosphorylatable 24 kDa subunit. The properties of both enzyme forms were found to be practically the same in respect to the substrate and phosphate donor specificities, kinetics, their sensitivity to heparin, etc. The results obtained strongly indicate that isolated yeast casein kinase II does not necessarily require the smallest subunit for the enzyme activity. |
| Databáze: | OpenAIRE |
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