The influence of a free α-ammonium group in the substrate upon trypsin-catalyzed transesterification
- 4 November 1969
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Enzymology
- Vol. 191 (2), 354-361
- https://doi.org/10.1016/0005-2744(69)90254-x
Abstract
No abstract availableThis publication has 11 references indexed in Scilit:
- Hydrophobic interactions of some alcohols with acyl trypsinsBiochimica et Biophysica Acta (BBA) - Enzymology, 1969
- Compétition nucléophile dans les réactions d'hydrolyse enzymatiqueEuropean Journal of Biochemistry, 1967
- Mise en evidence cinetique d'une transesterification au cours de l'hydrolyse trypsique de l'ester ethylique de la lysine en presence de divers alcoolsBiochimica et Biophysica Acta (BBA) - Enzymology, 1967
- Dielectric effects and transesterification reactions catalyzed by trypsinBiochimica et Biophysica Acta (BBA) - Enzymology, 1967
- Dielectric constant and enzyme kinetics solvent effects on the esterolytic activity of trypsinBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966
- The Kinetics of α-Chymotrypsin Reactions in the Presence of Added NucleophilesJournal of the American Chemical Society, 1964
- Effect of Ionic Strength on the Kinetics of Trypsin and Alpha ChymotrypsinThe Journal of general physiology, 1961
- THE INFLUENCE OF THE MEDIUM DIELECTRIC STRENGTH UPON TRYPSIN KINETICSThe Journal of general physiology, 1959
- DIELECTRIC CONSTANTS OF SOME ORGANIC SOLVENT-WATER MIXTURES AT VARIOUS TEMPERATURESJournal of the American Chemical Society, 1932
- THE APPARENT DISSOCIATION CONSTANTS OF ARGININE AND OF LYSINE AND THE APPARENT HEATS OF IONIZATION OF CERTAIN AMINO ACIDSPublished by Elsevier ,1930