In vivo phosphorylation of a synthetic peptide substrate of cyclic AMP-dependent protein kinase.
- 1 January 1978
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 75 (1) , 248-251
- https://doi.org/10.1073/pnas.75.1.248
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 phosphorylated in vivo after microinjection into Xenopus laevis oocytes. This result demonstrates that the microinjection technique, utilizing a synthetic peptide substrate, or possibly a synthetic substrate analog inhibitor 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.This publication has 26 references indexed in Scilit:
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