ELECTROMAGNETIC RADIATION CHEMISTRY.
Annual progress rept. no. 1, 15 Mar-15 Nov 63,
LOUISVILLE UNIV KY
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The initial discovery by others of an activation of the proteolytic enzyme trypsin by exposure to a magnetic field has been reinvestigated and confirmed. Changes were made in the experimental procedure, particularly in the analytical techniques, to render the results more accurate and reproducible. The enhancement in the activity consistently ranged from 10 to 23 for exposures of 1 to 3 hours in a field of 5 kilogauss. Formation of a complex between vitamin A aldehyde and antimony trichloride SbCl3 and the apparent isomerization of the geometrical isomers to one configuration was investigated. The nuclear magnetic resonance spectra of the all trans and the 13-cis isomers of vitamin A aldehyde were compared with the nmr spectra of these two isomers after reaction with SbCl3. The spectrum of the all-trans isomer is the same before and after the reaction. The 13-cis vitamin A aldehyde-SbCl3 product has a spectrum identical with that of the all trans isomer. The all trans aldehyde-SbCl3 has an electron paramagnetic resonance spectrum which consists of one broad single line supporting the idea of an ionic salt formation or charge transfer complex. Author