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RNA‐binding protein kinase from amphibian oocytes is a casein kinase II
Author(s) -
Kandror K.V.,
Stepanov A.S.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81363-0
Subject(s) - casein kinase 2 , protein kinase a , biochemistry , mitogen activated protein kinase kinase , c raf , cyclin dependent kinase 9 , casein kinase 1 , map2k7 , casein kinase 2, alpha 1 , proteases , chemistry , cyclin dependent kinase 2 , protein kinase r , biology , kinase , microbiology and biotechnology , enzyme
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.