期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1978
卷号：75
期号：1
页码：248-251
DOI：10.1073/pnas.75.1.248
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
