RNA‐binding protein kinase from amphibian oocytes is a casein kinase II

FEBS Letters

Stepanov, A.S.¹  Kandror, K.V.¹ 

[1] A.N. Bakh Institute of Biochemistry, USSR Academy of Sciences, Leninsky pr. 33, Moscow 117071, USSR

关键词: Amphibian oocyte;    tRNA-binding protein;    Cyclic AMP-independent protein kinase;    Phosphatase;    Protease;   

DOI  :  10.1016/0014-5793(84)81363-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

RNA-binding protein kinase from amphibian oocytes modifies serine and threonine residues in the molecules of substrates and utilizes both ATP and GTP. Low concentrations of heparin inhibit protein kinase. The foregoing suggests that this enzyme is casein kinase II. It is shown that RNA-binding proteins lack active forms of phosphatases and proteases which may affect the results of phosphorylation of both endogenous and exogenous substrates.

【 授权许可】

Unknown