The role of surface charge and hydrophobic interaction in the activation of rat liver adenylate cyclase
| Autor: | B Rubalcava, J A Pliego, J Cerbon, M O Grajales |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Male
Tetracaine Surface Properties Biophysics Adenylate kinase Receptors Cell Surface Stimulation Glucagon binding Biochemistry Glucagon Cyclase Fluorides Procaine Receptors Glucagon medicine Animals Anesthetics Local Molecular Biology Chemistry Cell Membrane Lidocaine Rats Inbred Strains Rats Enzyme Activation Kinetics Liver Cyclase activity Adenylyl Cyclases medicine.drug |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 759:243-249 |
| ISSN: | 0304-4165 |
| DOI: | 10.1016/0304-4165(83)90319-7 |
| Popis: | Rat liver plasma membranes were incubated either with procaine, lidocaine or tetracaine to study the binding of glucagon to receptors and the responses of adenylate cyclase to glucagon or fluoride. Procaine treatment increased the glucagon and fluoride activation of the cyclase and the stimulation was concentration-dependent; this compound seemed to act at the G/F unit level since changes in the glucagon binding were not observed and the basal activity was not modified. Tetracaine inhibited the adenylate cyclase activity in the order glucagon greater than basal greater than fluoride; it seems that tetracaine acted at the receptor unit level since it reduced the binding affinity. Tetracaine at high concentration (10 mM) also inhibited the fluoride stimulation of the Lubrol PX-solubilized enzyme; apparently the anesthetic acts on the G/F unit and this would indicate the component is still bound to the catalytic unit. The solubilized enzyme is not longer stimulated by procaine. These data suggested that the F component site of the G/F units is in some aspects different to the G component and more resistant to the detergent. The results of this work allowed a clear distinction among the different components of the glucagon-stimulated adenylate cyclase system and showed the importance of surface charge and hydrophobic interactions as regulatory mechanisms. |
| Databáze: | OpenAIRE |
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