Guanine nucleotides protect adenylate cyclase against inhibition by Pb2+ |
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| Authors: | Stein Ove Døskeland |
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| Affiliation: | Cell Biology Research Group, Preclinical Institutes, University of Bergen, Arstadveien 19, N-5000 Bergen, Norway |
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| Abstract: | The inhibition of rat liver adenylate cyclase (ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1) by Pb2+ could be separated into an irreversible and a reversible component.Evidence was obtained that both types of inhibition were due to free Pb2+, rather than Pb/ATP, and that Pb2+ did not act via the site wherein Mg2+ and Mn2+ activate the cyclase.Guanine nucleotides strongly counteracted the reversible inhibition of cyclase by Pb2+, providing onother example of guanine nucleotide effects on adenylate cyclase function.It is suggested that the Pb2+-inhibited cyclase may be of value in the study of guanine nucleotide-cyclase interactions. |
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| Keywords: | Guanine nucleotide Adenylate cyclase (Rat liver) App(NH)p, adenyl-5′-yl imidodiphosphate Gpp(NH)p, guanyl-5′-yl imidophosphate EGTA, ethane-dioxybis (ethylamine) tetraacetic acid |
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