{"doi":"10.1042/bj1830589","title":"Specificity for guanine nucleotide activation and stabilization of rabbit cardiac adenylate cyclase","abstract":"<jats:p>These studies examined the structural specificity for guanine nucleotide-facilitated hormonal activation and guanine nucleotide stabilization of cardiac adenylate cyclase. 1. The phosphonate analogues of GTP, p[CH2]ppG (guanosine 5′-[βγ-methylene]-triphosphate) and pp[CH2]pG (guanosine 5′-[αβ-methylene]triphosphate), were the most effective activators of adenylate cyclase. Other nucleotides producing significant activation (P&amp;lt;0.01) were, in decreasing order of activation: ITP, GDP, GMP, GTP, XTP, CTP, p[NH]ppG (guanosine 5′-[βγ-imido]triphosphate), dGTP and 2′-O-methyl-GTP. Guanosine, cyclic GMP, UTP and ppppG (guanosine tetraphosphate) had no effect, and 7-methyl-GTP caused a decrease in the activity. 2. Preincubation of membranes at 37°C for 15min before assay at 24°C produced an 80% decrease in adenylate cyclase activity, and preincubation with p[CH2]ppG and pp[CH2]pG protected and resulted in a net increase in activity. Other nucleotides that completely or partially preserved activity in decreasing order of effectiveness were p[NH]ppG, GDP, GTP, dGTP, ITP, ppppG, 2′-O-methyl-GTP, GMP, CTP and XTP. Several compounds had no effect, including guanosine, cyclic GMP and UTP, whereas preincubation with 7-methyl-GTP produced a further decrease (P&amp;lt;0.05) in activity. 3. The concentration-dependence for activation and stabilization by the naturally occurring guanine nucleotides was examined in the absence of a regenerating system and revealed GMP to have no stabilizing effect and to be less potent than either GDP or GTP in activating adenylate cyclase. 4. A significant correlation (r=0.90) was found between the properties of activation and stabilization for the compounds examined. These findings are consistent with there being a single nucleotide site through which both the activation and stabilization of adenylate cyclase are mediated.</jats:p>","journal":"Biochemical Journal","year":1979,"id":46029,"datarank":0.6319539072353524,"base_score":1.791759469228055,"endowment":1.791759469228055,"self_citation_contribution":0.26876392038420827,"citation_network_contribution":0.3631899868511441,"self_endowment_contribution":0.26876392038420827,"citer_contribution":0.3631899868511441,"corpus_percentile":null,"corpus_rank":null,"citation_count":5,"citer_count":5,"citers_with_citation_signal":4,"citers_with_endowment":4,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":214028,"name":"Robert J. 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