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

James L. Maller | Zendy; Bruce E. Kemp | Zendy; E G Krebs | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

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

Author(s) -

James L. Maller,

Bruce E. Kemp,

E G Krebs

Publication year - 1978

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.75.1.248

Subject(s) - phosphorylation , protein kinase a , dephosphorylation , peptide , biochemistry , kinase , phosphotransferase , cyclin dependent kinase 2 , protein phosphorylation , xenopus , biology , chemistry , mitogen activated protein kinase kinase , phosphatase , gene

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research