Intrinsic activity of guanosine 3',5'-monophosphate-dependent protein kinase similar to adenosine 3',5'-monophosphate-dependent protein kinase. II. Phosphorylation of ribosomal proteins.

Abstract:

:Guanosine 3',5'-monophosphate (cyclic GMP)-dependent protein kinase purified from silkworm pupae reacts with rat liver ribosomal proteins when a stimulatory modulator (Kuo, W.N. & Kuo, J.F. 1976) J. Biol. Chem. 251, 4283-4286) is added to the reaction mixture. Judging from autoradiogram of the radioactive proteins separated by electrophoresis on sodium dodecyl sulfate-polyacrylamide slab gel, the protein kinase utilizes the same proteins as those phosphorylated by adenosine 3',5'-monophosphate (cyclic AMP)-dependent protein kinase. Fingerprint maps of the tryptic phosphopeptides of radioactive ribosomal proteins, which are phosphorylated by these two classes of protein kinases, are very similar. These results suggest that cyclic GMP-dependent protein kinase possesses an intrinsic activity that is similar to that of cyclic AMP-dependent protein kinase.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Chihara-Nakashima M,Hashimoto E,Nishizuka Y

doi

10.1093/oxfordjournals.jbchem.a131648

subject

Has Abstract

pub_date

1977-06-01 00:00:00

pages

1863-7

issue

6

eissn

0021-924X

issn

1756-2651

journal_volume

81

pub_type

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