Abstract
Commercially available crystalline yeast alcohol dehydrogenase contained protein kinase activity. Casein and phosvitin were readily phosphorylated, but whole calf thymus histone was not. The protein kinase activity was inhibited by KCl, was not stimulated by cyclic AMP and could be separated from the alcohol dehydrogenase activity by sucrose density centrifugation.
Full text
PDFSelected References
These references are in PubMed. This may not be the complete list of references from this article.
- Chen L. J., Walsh D. A. Multiple forms of hepatic adenosine 3':5'-monophosphate dependent protein kinase. Biochemistry. 1971 Sep 14;10(19):3614–3621. doi: 10.1021/bi00795a020. [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]
- KAGI J. H., VALLEE B. L. The role of zinc in alcohol dehydrogenase. V. The effect of metal-binding agents on thestructure of the yeast alcohol dehydrogenase molecule. J Biol Chem. 1960 Nov;235:3188–3192. [PubMed] [Google Scholar]
- Kuo J. F., Greengard P. Cyclic nucleotide-dependent protein kinases. IV. Widespread occurrence of adenosine 3',5'-monophosphate-dependent protein kinase in various tissues and phyla of the animal kingdom. Proc Natl Acad Sci U S A. 1969 Dec;64(4):1349–1355. doi: 10.1073/pnas.64.4.1349. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Linn T. C., Pettit F. H., Reed L. J. Alpha-keto acid dehydrogenase complexes. X. Regulation of the activity of the pyruvate dehydrogenase complex from beef kidney mitochondria by phosphorylation and dephosphorylation. Proc Natl Acad Sci U S A. 1969 Jan;62(1):234–241. doi: 10.1073/pnas.62.1.234. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Murray A. W., Froscio M. Cyclic adenosine 3':5'-monophosphate and microtubule function: specific interaction of the phosphorylated protein subunits with a soluble brain component. Biochem Biophys Res Commun. 1971 Sep;44(5):1089–1095. doi: 10.1016/s0006-291x(71)80197-3. [DOI] [PubMed] [Google Scholar]
- RABINOWITZ M., LIPMANN F. Reversible phosphate transfer between yolk phosphoprotein and adenosine triphosphate. J Biol Chem. 1960 Apr;235:1043–1050. [PubMed] [Google Scholar]
- Reimann E. M., Walsh D. A., Krebs E. G. Purification and properties of rabbit skeletal muscle adenosine 3',5'-monophosphate-dependent protein kinases. J Biol Chem. 1971 Apr 10;246(7):1986–1995. [PubMed] [Google Scholar]
- Sy J., Richter D. Separation of a cyclic 3',5'-adenosine monophosphate binding protein from yeast. Biochemistry. 1972 Jul 18;11(15):2784–2787. doi: 10.1021/bi00765a008. [DOI] [PubMed] [Google Scholar]
- WILLIAMS J., SANGER F. The grouping of serine phosphate residues in phosvitin and casein. Biochim Biophys Acta. 1959 May;33(1):294–296. doi: 10.1016/0006-3002(59)90545-1. [DOI] [PubMed] [Google Scholar]