A two-state model of an enzyme with an allosteric regulatory site capable of metabolizing the regulatory ligand. Simplified mathematical treatments of transient and steady state kinetics of an activator and its competitive inhibition as applied to adenylyl cyclases.
Open Access
- 1 April 1980
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 255 (8) , 3552-3557
- https://doi.org/10.1016/s0021-9258(19)85736-8
Abstract
No abstract availableThis publication has 6 references indexed in Scilit:
- Allosteric proteins and cellular control systemsPublished by Elsevier ,2009
- Transient and steady state kinetics of the interaction of guanyl nucleotides with the adenylyl cyclase system from rat liver plasma membranes. Interpretation in terms of a simple two-state model.Journal of Biological Chemistry, 1980
- Slow Transitions and Hysteretic Behavior in EnzymesAnnual Review of Biochemistry, 1979
- Mechanism of adenylate cyclase activation by cholera toxin: Inhibition of GTP hydrolysis at the regulatory siteProceedings of the National Academy of Sciences, 1977
- Catecholamine-stimulated GTPase activity in turkey erythrocyte membranesBiochimica et Biophysica Acta (BBA) - Enzymology, 1976
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965