Characterization of phosphorylase kinase activities in yeast.
Biochem Biophys Res Commun
; 114(1): 331-8, 1983 Jul 18.
Article
en En
| MEDLINE
| ID: mdl-6309169
Two phosphorylase kinase activities were resolved by DEAE-cellulose chromatography. The main activity peak was enriched 2800-fold, the minor appeared to be an aggregate of the enzyme. Phosphorylase kinase also phosphorylated histone and casein with no changes in phosphorylation ratios throughout the preparation steps but was most active on yeast phosphorylase. The molecular weight was 29000 +/- 2000. ATP, UTP, GTP served as substrates while CTP was inactive. Mg-ions activated the kinase without inhibition at high concentrations (30 mM). In addition to this cAMP-independent kinase, cAMP-dependent protein kinase also phosphorylated phosphorylase. The catalytic subunit and phosphorylase kinase were not identical since the latter was not inhibited by yeast cAMP binding protein.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fosforilasa Quinasa
/
Saccharomyces cerevisiae
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
1983
Tipo del documento:
Article
Pais de publicación:
Estados Unidos