ELECTROMAGNETIC RADIATION CHEMISTRY.
Abstract
An investigation of the interaction of the enzyme trypsin with magnetic fields was undertaken. It appears that under the conditions studied there is no detectable magnetic effect on the activity of this enzyme. ESR was used to determine structural changes which might be induced in copper II-trypsin solutions on exposure to magnetic fields of 14,000 gauss. The bonding parameter alpha square was evaluated for several amino acid, peptide and trypsin complexes with copper II ions at liquid nitrogen temperatures. The changes in the nature of the metal to ligand bonding is reflected in changing values of alpha square as the pH is varied. There appears to be a reasonable correlation between those structures proposed in the literature as determined by spectrophotometric and potentiometric techniques and the values of alpha square as determined from esr measurements. Of particular interest is the marked change in the nature of the bonding in the trypsin--copper II complex over the range pH 5-6, which suggests a notable rearrangement from primarily carboxylate bonding sites to amide and amine bonding sites. There does not appear to be any detectable change in esr parameters on exposure of trypsin-copper II samples to magnetic fields of approximately 14,000 gauss. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 31, 1966
- Accession Number
- AD0646645
Entities
People
- Thomas H. Crawford
Organizations
- University of Louisville