The inhibitory effect of methanol on forskolin-activated adenylate cyclase in rat erythrocyte membranes dependent on the state of the guanine nucleotide-binding stimulatory and regulatory protein.
- 1 January 1988
- journal article
- research article
- Published by Pharmaceutical Society of Japan in Journal of Pharmacobio-Dynamics
- Vol. 11 (5) , 377-380
- https://doi.org/10.1248/bpb1978.11.377
Abstract
Forskolin-activated adenylate cyclase activity in rat erythrocyte membranes was markedly inhibited by methanol in a concentration dependent manner. On the contrary, no change was observed in the basal cyclase activity in the presence of methanol. The methanol inhibition forskolin-activated cyclase activity was protected by the stimulation of Gs in the presence of NaF in a concentration dependent manner. These data indicate that low- and high-affinity binding sites of forskolin in rat erythrocyte membranes have different sensitivities to methanol.This publication has 2 references indexed in Scilit:
- Forskolin stabilizes a functionally coupled state between activated guanine nucleotide-binding stimulatory regulatory protein, Ns, and catalytic protein of adenylate cyclase system in rat erythrocytesBiochemical and Biophysical Research Communications, 1986
- Regulation of adenylate cyclase of human platelet membranes by forskolin.Journal of Biological Chemistry, 1982