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- W1917754756 abstract "A single cAMP-receptor protein could be detected in mycelial extracts of Coprinun macrorhizus by using the photoaffinity cAMP-analogue, 8-N3-cAMP. The protein which specifically bound 32P-labeled 8-N3-cAMP had an apparent molecular weight of 46,000 as determined by an SDS-polyacrylamide gel electrophoresis system. The 46,000-dalton protein was characterized by the dissociation constant for [32P]-8-N3-cAMP, and by the nucleotide specific inhibition of [32P]-8-N3-cAMP binding. The 46,000-dalton protein was co-chromatographed on a DEAE-cellulose column with cAMP-dependent protein kinase. The levels of [32P]-8-N3-cAMP-binding and protein kinase activities in mycelial extracts of strains used was always in parallel. The result indicated that the 46,000-dalton protein may be a regulatory subunit of protein kinase with the capacity to bind cAMP. cAMP-dependent protein kinase of this fungus was immunologically different from those of higher animals." @default.
- W1917754756 created "2016-06-24" @default.
- W1917754756 date "1981-04-01" @default.
- W1917754756 modified "2023-09-25" @default.
- W1917754756 title "Adenosine 3', 5'-Monophosphate-Receptor Protein and Protein Kinase in <italic>Coprinus macrorhizus</italic>" @default.
- W1917754756 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a133313" @default.
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