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Activation of Skeletal Muscle Phosphorylase Kinase by Adenosine Triphosphate and Adenosine 3′,5′-Monophosphate
Open accessAbstract
Abstract Rabbit skeletal muscle phosphorylase kinase has been obtained as a nearly homogeneous protein showing a single peak on electrophoresis and in the ultracentrifuge. Incubation of the purified kinase with γ32P-ATP in the presence of Mg++ ions activates the enzyme; this process is accompanied by phosphorylation of the protein. Activation and phosphorylation of phosphorylase kinase occur more rapidly when cyclic 3',5'-AMP or glycogen is present in activation reaction mixtures, but these two substances apparently act by different mechanisms since their effects are additive. Cyclic 3',5'-AMP and glycogen stimulate activation of the kinase more than they affect phosphorylation. No evidence was obtained to indicate that cyclic 3',5'-AMP undergoes any modification when it exerts its effect on phosphorylase kinase activation. Activation of the kinase was shown to be autocatalytic, but the possibility that cyclic 3',5'-AMP acts through stimulation of a second enzyme involved in the system was suggested by the failure to find any evidence for a significant degree of binding of this nucleotide to purified phosphorylase kinase.
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Citations
Cited by
An Adenosine 3′,5′-Monophosphate-dependant Protein Kinase from Rabbit Skeletal Muscle
Walsh, D. A., Perkins, J. P., & Krebs, E. G. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)34204-8 · Cited by 1,445
Self-citationCyclic Nucleotide-dependent Protein Kinases
Miyamoto, E., Kuo, J. F., & Greengard, P. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63478-7 · Cited by 548
PKC and the control of localized signal dynamics
Rosse, C., Linch, M., Kermorgant, S., Cameron, A. J. M., Boeckeler, K., & Parker, P. J. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2847 · Cited by 477
Lisman, J. E. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.9.3055 · Cited by 475
The control of glycogen metabolism in the liver
Hers, H. G., De Wulf, H., & Stalmans, W. (1970) · FEBS Letters · doi:10.1016/0014-5793(70)80569-5 · Cited by 414
Metadata
- Authors
- DeLange, R. J., Kemp, R. G., Riley, W. D., Cooper, R. A., & Krebs, E. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1968-05
- Volume
- 243
- Issue
- 9
- Pages
- 2200-2208
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1605839106
- Cited by
- 328
- References
- 0
- FWCI
- 15.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- DeLange, R. J., Kemp, R. G., Riley, W. D., Cooper, R. A., & Krebs, E. G. (1968). Activation of Skeletal Muscle Phosphorylase Kinase by Adenosine Triphosphate and Adenosine 3′,5′-Monophosphate. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)93463-0
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