A test for the two-stage thermoinactivation model for chymotrypsin

This publication has 12 references indexed in Scilit:

• Heat inactivation of lipase from psychrotrophic Pseudomonas fluorescens P38: Activation parameters and enzyme stability at low or ultra-high temperatures
  Food Chemistry, 1992
• The effect of calcium on bovine α-lactalbumin conformational transitions by ultraviolet difference and fluorescence spectrophotometry
  Food Chemistry, 1992
• Contribution of the hydrophobic effect to globular protein stability
  Journal of Molecular Biology, 1992
• A kinetic and equilibrium study of the denaturation of aspartic proteinases from the fungi, Endothia parasitica and Mucor miehei
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
• Analysis of Processes Causing Thermal Inactivation of Enzymes
  Published by Wiley ,1988
• Reaction Kinetics of the Denaturation of Whey Proteins in Milk
  Journal of Food Science, 1988
• Characterization of the transition state of Lysozyme unfolding. I. Effect of protein‐solvent interactions on the transition state
  Biopolymers, 1984
• Structure-stability relationships in proteins: new approaches to stabilizing enzymes
  Enzyme and Microbial Technology, 1984
• On the mechanism of irreversible thermoinactivation of enzymes and possibilities for reactivation of “irreversibly” inactivated enzymes
  Biochemical and Biophysical Research Communications, 1978
• Urea and Guanidine Hydrochloride Denaturation of Ribonuclease, Lysozyme, α-Chymotrypsin, and b-Lactoglobulin
  Journal of Biological Chemistry, 1974