Cooperativity and the slow isomerization of δ-chymotrypsin
- 1 April 1979
- journal article
- research article
- Published by Springer Nature in Molecular and Cellular Biochemistry
- Vol. 24 (3) , 183-191
- https://doi.org/10.1007/bf00220737
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- Cooperativity and slow transitions in the regulation of oligomeric and monomeric enzymesTrends in Biochemical Sciences, 1976
- Allosteric Activation of the Hydrolysis of Specific Substrates by ChymotrypsinEuropean Journal of Biochemistry, 1976
- The Conformational Oscillation of delta-Chymotrypsin Involvement of Methionine-192European Journal of Biochemistry, 1975
- The Time Dependence of the Activity of δ‐Chymotrypsin at High pHEuropean Journal of Biochemistry, 1973
- Transients and cooperativity. A slow transition model for relating transients and cooperative kinetics of enzymes.1972
- Transients and CooperativityJournal of Biological Chemistry, 1972
- Conformational equilibria in α- and δ-chymotrypsin: The energetics and importance of the salt bridgeJournal of Molecular Biology, 1972
- Binding of competitive inhibitors to δ-chymotrypsin in the alkaline pH region. Competitive inhibition kinetics and proton-uptake measurementsBiochemistry, 1970
- The Statistical Analysis of Enzyme Kinetic DataPublished by Wiley ,1967