Related Experiment Video
Updated: Jun 19, 2026

Use of the Protease Fluorescent Detection Kit to Determine Protease Activity
Published on: August 4, 2009
THE EQUILIBRIUM BETWEEN ACTIVE NATIVE TRYPSIN AND INACTIVE DENATURED TRYPSIN
1Laboratories of The Rockefeller Institute for Medical Research, Princeton, N. J., and the Hospital of The Rockefeller Institute for Medical Research, New York.
The equilibrium between native and denatured trypsin is influenced by acid, alkali, alcohol, and temperature. The calculated heat of denaturation in hydrochloric acid is -67,600 calories per mole.
Area of Science:
- Biochemistry
- Protein Chemistry
Background:
- Trypsin is a key digestive enzyme.
- Protein denaturation is a critical process affecting enzyme function.
Purpose of the Study:
- To investigate the mobile equilibrium between native and denatured trypsin.
- To determine the thermodynamic parameters of trypsin denaturation.
Main Methods:
- Studying the effect of temperature on the equilibrium constant.
- Utilizing acid, alkali, and alcohol as denaturing agents.
Main Results:
- A mobile equilibrium exists between native and denatured trypsin.
- Factors influencing this equilibrium include acid, alkali, alcohol, and temperature.
- The heat of denaturation in 0.01 N hydrochloric acid was determined to be -67,600 calories per mole.
Conclusions:
- Trypsin's structural integrity is sensitive to environmental conditions.
- Understanding denaturation equilibrium is crucial for enzyme stability studies.
More Related Videos
19:16The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
Published on: March 17, 2010
11:27X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Related Concept Videos
Introduction to Mechanisms of Enzyme Catalysis
Enzymes
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Protein Denaturation
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Induced-fit Model
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
Catalytically Perfect Enzymes