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 Biochemjournal_title
Journal of biochemistryauthors
Chihara-Nakashima M,Hashimoto E,Nishizuka Ydoi
10.1093/oxfordjournals.jbchem.a131648subject
Has Abstractpub_date
1977-06-01 00:00:00pages
1863-7issue
6eissn
0021-924Xissn
1756-2651journal_volume
81pub_type
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