Slow GDP Dissociation from the guanyl nucleotide‐binding site of turkey erythrocyte membranes as the limiting step in the activation of adenylate cyclase by β‐adrenergic agonists
- 15 December 1979
- journal article
- Published by Wiley in FEBS Letters
- Vol. 108 (2), 365-368
- https://doi.org/10.1016/0014-5793(79)80565-7
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Mode of coupling between the β-adrenergic receptor and adenylate cyclase in turkey erythrocytesBiochemistry, 1978
- Mechanism of adenylate cyclase activation through the beta-adrenergic receptor: catecholamine-induced displacement of bound GDP by GTP.Proceedings of the National Academy of Sciences, 1978
- Structure-binding—Activity analysis of beta-adrenergic amines—IBiochemical Pharmacology, 1978
- Catecholamine-stimulated GTPase activity in turkey erythrocyte membranesBiochimica et Biophysica Acta (BBA) - Enzymology, 1976
- Synergistic activation of adenylate cyclase by guanylyl imidophosphate and epinephrineBiochemistry, 1976
- The control of adenylate cyclase by calcium in turkey erythrocyte ghosts.Journal of Biological Chemistry, 1975
- Activation of pigeon erythrocyte membrane adenylate cyclase by guanylnucleotide analogues and separation of a nucleotide binding protein.Journal of Biological Chemistry, 1975
- Stimulation by thyrotropin of horse thyroid plasma membranes adenylate cyclase: Evidence of cooperativityBiochemical and Biophysical Research Communications, 1974
- A new simple method for separation of adenosine 3′,5′-cyclic monophosphate from other nucleotides and its use in the assay of adenyl cyclaseAnalytical Biochemistry, 1971
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951