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. 1978 Jan;75(1):248–251. doi: 10.1073/pnas.75.1.248

In vivo phosphorylation of a synthetic peptide substrate of cyclic AMP-dependent protein kinase.

J L Maller, B E Kemp, E G Krebs
PMCID: PMC411223  PMID: 203933

Abstract

A model synthetic peptide substrate of the cyclic AMP-dependent protein kinase (ATP:protein phosphotransferase; EC 2.7.1.37), Leu-Arg-Arg-Ala-Ser-Leu-Gly, closely resembling the local phosphorylation site sequence in porcine hepatic pyruvate kinase, was shown to be phosphorylated in vivo after microinjection into Xenopus oocytes. This result demonstrates that the microinjection technique, utilizing a synthetic peptide substrate, or possibly a synthetic substrate analog inhibitor [Kemp, B. E., Benjamini, E. & Krebs, E. G. (1976) Proc. Natl. Acad. Sci. USA 73, 1038--1042], can be used to study protein phosphorylation-dephosphorylation reactions in living oocytes. This follows, since it is clear that the injected peptide was accessible to the cellular compartment containing the protein kinase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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