Two different intrachain cAMP binding sites of cAMP-dependent protein kinases.
作者： S.R. Rannels , J.D. Corbin
DOI: 10.1016/S0021-9258(20)79665-1
关键词:
摘要: The regulatory subunits of both isozymes cAMP-dependent protein kinase bind 2 mol cAMP/mol monomer. cAMP dissociation studies indicate similar binding behavior for each isozyme. Each has two different intrachain components present in approximately equal amounts and the rate is 5- to 10-fold slower from one site (Site 1) than other 2). Equilibrium [3H]cAMP inhibited by several competing cyclic nucleotides. Following equilibrium using saturating presence nucleotide, pattern release [3H]cAMP, monitored an excess nonradioactive cAMP, suggests site-specific selectivity some As compared with cIMP prefers Site subunits, whereas N6, O2-dibutyryl-cAMP shows a preference only isozyme II subunit. 8-Bromo-cAMP, 8-bromo-cGMP, 8-azido-cAMP prefer 1 proteins. results that sites have analogue specificities rates. or but not identical nucleotide specificity corresponding
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