Abstract
Myelin basic protein was shown to be a substrate for protein kinase from rabbit muscle. One of the major sites of phosphorylation was the serine residue in the sequence Gly-Arg-Gly-Leu-Ser-Leu. The arginine residue in this sequence is known to be a substrate for a protein methylase.
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Selected References
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- Baldwin G. S., Carnegie P. R. Specific enzymic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin. Science. 1971 Feb 12;171(3971):579–581. doi: 10.1126/science.171.3971.579. [DOI] [PubMed] [Google Scholar]
- Carnegie P. R. Amino acid sequence of the encephalitogenic basic protein from human myelin. Biochem J. 1971 Jun;123(1):57–67. doi: 10.1042/bj1230057. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Deibler G. E., Martenson R. E., Kies M. W. Large scale preparation of myelin basic protein from central nervous tissue of several mammalian species. Prep Biochem. 1972;2(2):139–165. doi: 10.1080/00327487208061467. [DOI] [PubMed] [Google Scholar]
- Glynn I. M., Chappell J. B. A simple method for the preparation of 32-P-labelled adenosine triphosphate of high specific activity. Biochem J. 1964 Jan;90(1):147–149. doi: 10.1042/bj0900147. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Johnson E. M., Maeno H., Greengard P. Phosphorylation of endogenous protein of rat brain by cyclic adenosine 3',5'-monophosphate-dependent protein kinase. J Biol Chem. 1971 Dec 25;246(24):7731–7739. [PubMed] [Google Scholar]
- Kemp B. E., Froscio M., Murray A. W. Protein kinase activity in commercially available crystalline yeast alcohol dehydrogenase. Biochem J. 1973 Feb;131(2):271–274. doi: 10.1042/bj1310271. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Krebs E. G. Protein kinases. Curr Top Cell Regul. 1972;5:99–133. [PubMed] [Google Scholar]
- Murray K., Milstein C. Esters of serine and threonine in hydrolysates of histones and protamines, and attendant errors in amino acid analyses of proteins. Biochem J. 1967 Nov;105(2):491–495. doi: 10.1042/bj1050491. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Trauch J. A., Mumby M., Traut R. R. Phosphorylation of ribosomal proteins by substrate-specific protein kinases from rabbit reticulocytes. Proc Natl Acad Sci U S A. 1973 Feb;70(2):373–376. doi: 10.1073/pnas.70.2.373. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Walsh D. A., Perkins J. P., Krebs E. G. An adenosine 3',5'-monophosphate-dependant protein kinase from rabbit skeletal muscle. J Biol Chem. 1968 Jul 10;243(13):3763–3765. [PubMed] [Google Scholar]
- Weller M., Rodnight R. Protein kinase activity in membrane preparations from ox brain. Stimulation of intrinsic activity by adenosine 3':5'-cyclic monophosphate. Biochem J. 1973 Mar;132(3):483–492. doi: 10.1042/bj1320483. [DOI] [PMC free article] [PubMed] [Google Scholar]
