The active site and mechanism of action of bovine pancreatic ribonuclease. 5. The charge types at the active centre
- 1 October 1962
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 85 (1) , 139-144
- https://doi.org/10.1042/bj0850139
Abstract
(1) The activity of ribonuclease can be enhanced or depressed by solvents depending on the pH and the nature of the buffer. (2) A general method of determining the charge types of the groups at the active site of an enzyme, based on the use of organic solvents, is presented and applied to ribonuclease. (3) The pH-activity curve of ribonuclease has been measured in water 50% (v/v) dioxan and 50% (v/v) formamide in cationic-acid and in neutral-acid buffers. (4) The active site of ribonuclease contains two groups whose acid species are cationic.This publication has 5 references indexed in Scilit:
- The active site and mechanism of action of bovine pancreatic ribonuclease. 4. The activity in inert organic solvents and alcoholsBiochemical Journal, 1962
- The active site and mechanism of action of bovine pancreatic ribonuclease. 3. The pH-dependence of the kinetic parameters for the hydrolysis of cytidine 2′,3′-phosphateBiochemical Journal, 1962
- [Influence of variations of pH and dielectric constant on the kinetics of hydrolysis of native beta-lactoglobulin by trypsin].1960
- The trypsin-catalyzed hydrolysis of benzoyl-l-arginine ethyl esterBiochimica et Biophysica Acta, 1960
- ANIONIC POLYMERS .2. INHIBITION OF RIBONUCLEASE1958