The effect of phosphorylation of the EF-2 isolated from rat liver cells on protein biosynthesis in vitro.
Acta Biochim Pol
; 38(3): 353-8, 1991.
Article
em En
| MEDLINE
| ID: mdl-1665936
ABSTRACT
The activity of EF-2 was distinctly decreased after phosphorylation catalysed by a partly purified calmodulin and Ca2+ dependent protein kinase III. At the same time 32P from [gamma-32P]ATP was incorporated into EF-2 molecule. After dephosphorylation of EF-2 catalysed by alkaline phosphatase the activity of this factor was increased. This suggests that the phosphorylation-dephosphorylation of EF-2 is the regulatory process in the elongation step of the translation. Preliminary purification of the kinase III from rat liver resulted in 8-fold purified enzyme with a recovery of 60%.
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Base de dados:
MEDLINE
Assunto principal:
Fosfoproteínas
/
Proteínas Ribossômicas
/
Fatores de Alongamento de Peptídeos
/
Fígado
Limite:
Animals
Idioma:
En
Revista:
Acta Biochim Pol
Ano de publicação:
1991
Tipo de documento:
Article
País de afiliação:
Polônia