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THE INACTIVATION OF TRYPSIN BY X-RAYS
1Laboratories of The Rockefeller Institute for Medical Research.
Soft x-rays inactivate trypsin, mirroring heat inactivation. This radiation effect, primarily on active trypsin, follows a monomolecular reaction law, suggesting ionization is the key factor.
Area of Science:
- Biochemistry
- Radiation Biology
- Enzymology
Background:
- Trypsin is a crucial digestive enzyme.
- Understanding enzyme inactivation mechanisms is vital for various applications.
- Previous studies explored radiation effects on biological molecules.
Purpose of the Study:
- To investigate the inactivating effects of soft x-rays on trypsin.
- To compare x-ray inactivation with spontaneous heat inactivation.
- To elucidate the mechanism of trypsin inactivation by radiation.
Main Methods:
- Studying trypsin solutions at different concentrations.
- Exposing trypsin to soft x-ray radiation of constant intensity.
- Measuring enzyme activity to quantify inactivation.
- Comparing experimental results with existing data on beta-ray inactivation.
Main Results:
- Soft x-ray inactivation of trypsin parallels spontaneous heat inactivation.
- Inactivation is primarily observed in free or active trypsin.
- Trypsin inactivation follows a monomolecular reaction law under constant radiation intensity.
- Ionization is identified as the primary mechanism responsible for inactivation.
Conclusions:
- Soft x-ray radiation inactivates trypsin through a process similar to heat inactivation.
- The inactivation mechanism is dependent on ionization, likely involving electrical neutralization of the trypsin ion.
- The findings support the hypothesis that ionization is the sole determinant of radiation-induced enzyme inactivation.
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