PHYSICO-CHEMICAL INVESTIGATION OF THE MECHANISM OF ENZYME INACTIVATION. PART III. THERMODYNAMIC ANALYSIS OF STRUCTURAL AND CHEMICAL CHANGES IN PROTEIN DURING RADIATION INACTIVATION
Abstract
A method for studying the structural and chemical changes during the individual stages of the radiation inactivation of enzymes is proposed, which consists of applying the Eyring-Stearn method of thermodynamic analysis of protein denaturing to the thermal radiation after-effect reaction. It was shown by this method that in the process of formation of latent damage in the myosin and pepsin molecules 10-15 hydrogen bonds are ruptured, but the covalent bonds are not ruptured; in the second stage of inactivation -- upon realization of the latent damage -- the rupture of one covalent bond (apparently the disulfide bond) and 3-4 hydrogen bonds takes place. The hypothesis is expressed that the rupture of the hydrogen bonds in the first stage of inactivation takes place due to the Platzman-Franck polarization effect, but only after preliminary migration and localization of the charge at 'weak' sites of the structure, particularly at the S-S bridges. 'Fusion' of sections of the protein molecule in this region during the first stage of inactivation guarantees the possibility of carrying out the second stage.
Document Details
- Document Type
- Technical Report
- Publication Date
- Oct 17, 1967
- Accession Number
- AD0677828
Entities
People
- L. Kh. Eidus
Organizations
- United States Army Biological Warfare Laboratories