RNA‐binding protein kinase from amphibian oocytes is a casein kinase II
- 7 May 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 170 (1) , 33-37
- https://doi.org/10.1016/0014-5793(84)81363-0
Abstract
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.Keywords
This publication has 14 references indexed in Scilit:
- Inhibition of rat liver cytosol casein kinases by heparinFEBS Letters, 1982
- Protein kinase activity in RNA‐binding proteins of Amphibia oocytesFEBS Letters, 1982
- Purification and characterization of cytoplasmic protamine messenger ribonucleoprotein particles from rainbow trout testis cellsBiochemistry, 1982
- Identification of Casein Kinase II and Phosphorylated Proteins Associated with Messenger Ribonucleoproteins Particles from ReticulocytesEuropean Journal of Biochemistry, 1982
- Protein Kinases and Their Protein Substrates in Free Messenger Ribonucleoprotein Particles and Polysomes from Mouse Plasmacytoma CellsEuropean Journal of Biochemistry, 1981
- Selective inhibition of a cyclic nucleotide‐independent protein kinase (G‐type casein kinase) by naturally occurring glycosaminoglycansFEBS Letters, 1980
- Control of ribosomal protein phosphorylation in HeLa cellsBiochemical and Biophysical Research Communications, 1980
- Presence of Cyclic‐AMP‐Independent Protein Kinase Activity in RNA‐Binding Proteins of Embryonic Chicken MuscleEuropean Journal of Biochemistry, 1980
- A rapid, sensitive, and specific method for the determination of protein in dilute solutionAnalytical Biochemistry, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970