Subsites and catalytic mechanism of ribonuclease T1: kinetic studies using GpA, GpC, GpG, and GpU as substrates
- 1 October 1978
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 17 (20), 4124-4130
- https://doi.org/10.1021/bi00613a003
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Ribose recognition by ribonuclease T1: difference spectral binding studies with guanosine and deoxyguanosineBiochemistry, 1976
- Titration properties of homodinucleoside monophosphates. Determination of overlapping ionization constants and intramolecular stacking equilibrium quotients of ApA, CpC, GpG, and UpUJournal of the American Chemical Society, 1976
- Subsites and catalytic mechanism of ribonuclease T1: Kinetic studies using GpC and GpU as substratesArchives of Biochemistry and Biophysics, 1976
- Subsite interactions of ribonuclease T1: binding studies of dimeric substrate analogsBiochemistry, 1976
- A general purpose curve fitting program for class and research useJournal of Chemical Education, 1971
- 6 The Structure of ChymotrypsinPublished by Elsevier ,1971
- The Identification of a Glutamic Acid Residue as Part of the Active Site of Ribonuclease T1Journal of Biological Chemistry, 1967
- MULTIPLE INTERMEDIATES IN STEADY STATE ENZYME KINETICS .5. EFFECT OF PH ON RATE OF A SIMPLE ENZYMATIC REACTION1963
- Statistical estimations in enzyme kineticsBiochemical Journal, 1961
- The effect of pH on the affinities of enzymes for substrates and inhibitorsBiochemical Journal, 1953