Døskeland S O
Biochim Biophys Acta. 1980 Jun 5;630(1):15-21. doi: 10.1016/0304-4165(80)90132-4.
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 another 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.
Pb2+对大鼠肝脏腺苷酸环化酶（ATP焦磷酸裂解酶（环化），EC 4.6.1.1）的抑制作用可分为不可逆和可逆两个部分。有证据表明，这两种抑制类型均归因于游离的Pb2+，而非Pb/ATP，并且Pb2+并非通过Mg2+和Mn2+激活环化酶的位点起作用。鸟嘌呤核苷酸强烈对抗Pb2+对环化酶的可逆抑制作用，这为鸟嘌呤核苷酸对腺苷酸环化酶功能的影响提供了另一个例子。有人提出，受Pb2+抑制的环化酶可能在鸟嘌呤核苷酸-环化酶相互作用的研究中具有价值。
