A Thermodynamic Study of the Hydrolysis of Cytidine 2‘,3‘-Cyclic Phosphate
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference25 articles.
1. 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′-phosphate
2. The pH-rate profile of the ribonuclease-catalysed hydrolysis of cytidine 2′,3′-cyclic phosphate
3. Anionic Polymers
4. Relaxation Spectra of Ribonuclease. I. The Interaction of Ribonuclease with Cytidine 3′-Phosphate
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1. Deciphering the Mechanism of RNase T1;Methods in Enzymology;2001
2. Physicochemical characterization and in vitro interaction with brain capillary endothelial cells of artificially monoacylated ribonucleases A;Letters in Peptide Science;1997-12
3. The enthalpy changes upon hydrolysis of guanosine triphosphate anhydride and ester bonds;Archives of Biochemistry and Biophysics;1981-11
4. Micellar solubilization of enzymes in hydrocarbon solvents, enzymatic activity and spectroscopic properties of ribonuclease in n-octane;Biochemical and Biophysical Research Communications;1979-07
5. The enthalpies of hydrolysis of acyclic, monocyclic, and glycoside cyclic phosphate diesters.;Journal of Biological Chemistry;1975-07
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