Adenosine 3',5'-monophosphate-receptor protein and protein kinase in Coprinus macrorhizus.

摘要: A single cAMP-receptor protein could be detected in mycelial extracts of Coprinun macrorhizus by using the photoaffinity cAMP-analogue, 8-N3-cAMP. The which specifically bound 32P-labeled 8-N3-cAMP had an apparent molecular weight 46,000 as determined SDS-polyacrylamide gel electrophoresis system. 46,000-dalton was characterized dissociation constant for [32P]-8-N3-cAMP, and nucleotide specific inhibition [32P]-8-N3-cAMP binding. co-chromatographed on a DEAE-cellulose column with cAMP-dependent kinase. levels [32P]-8-N3-cAMP-binding kinase activities strains used always parallel. result indicated that may regulatory subunit capacity to bind cAMP. this fungus immunologically different from those higher animals.