Abstract
Crystalline soybean trypsin inhibitor protein undergoes denaturation on heating which is reversed on cooling. In the range of temperature of 35 to 50°C. a solution of the protein consists of a mixture of native and denatured forms in equilibrium with each other. The equilibrium is only slowly established and its final value at any temperature is the same whether a heated, denatured solution of the protein is cooled to the given temperature or whether a fresh solution is raised to that temperature. The kinetics of reversible denaturation of the soybean protein as well as the reversal of denaturation is that of a reversible unimolecular reaction, each process consisting at a given temperature of the same two simultaneous reactions acting in opposite directions. The experimental data on the effect of temperature on the velocity and the equilibrium constants of the opposing reaction were utilized in evaluating the reaction energies and activation energies. The reaction energies for denaturation were found to be as follows:— Change in total heat of reaction ΔH = 57,000 calories per mole Change in entropy of reaction ΔS = 180 calories per degree per mole The heat of activation ΔH 1 ‡ for denaturation = 55,000 The heat of activation ΔH 2 ‡ for the reversal of denaturation = –1900 The entropy ΔS 1 ‡ for denaturation = 95 The entropy ΔS 2 ‡ for reversal of denaturation = –84
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Selected References
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- Kunitz M. CRYSTALLIZATION OF A TRYPSIN INHIBITOR FROM SOYBEAN. Science. 1945 Jun 29;101(2635):668–669. doi: 10.1126/science.101.2635.668. [DOI] [PubMed] [Google Scholar]
- Pace J. The inactivation of trypsin by heat. Biochem J. 1930;24(3):606–614. doi: 10.1042/bj0240606. [DOI] [PMC free article] [PubMed] [Google Scholar]