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ELECTRON-SPIN RESONANCE STUDIES OF BOVINE-SERUM ALBUMIN AND CYSTINE IRRADIATED WITH $gamma$-RAYS AT 77 K AND AT ROOM TEMPERATURE

Journal Article · · Intern. J. Radiation Biol.
OSTI ID:4803517
Previous investigations at room temperature have shown that irradiated proteins, in general, give rise to only two types of resonanee pattern. One of these is asymmetric and similar to that of cystine. This similarity has led to the postulate that unpaired electrons formed within the protein migrate to the sulfur atoms of the cystine residue. It is found that the ESR spectrum obtained with BSA after irradiation in vacuum and examination at 77 deg K is different from that obtained on warming to room temperature. That observed on warming to room tenmperature is qualitatively the same as that obtained after irradiation in vacuum at room temperature, although the concentration of radicals in this latter case is greater. With cystine the ESR pattern obtained after irradiation in a vacuum and examination at 77 deg K is different from that obtained on warming to room temperature. This radical observed on warming to room temperature is very stable and is also produced after irradiation in vacuum at room temperature. It is unaffected by oxygen. While at room temperature the signals from cystine and BSA show some similarities, the spectra are quite different at 77 deg K, which reflects the primary radiation processes uncomplicated by secondary processes. The work does not support the contention that the radicals produced have a high probability of migrating to the sulfur atoms. (auth)
Research Organization:
Royal Military Coll. of Science, Shrivenham, nr. Swindon, Wiltshire, Eng.
NSA Number:
NSA-16-012896
OSTI ID:
4803517
Journal Information:
Intern. J. Radiation Biol., Journal Name: Intern. J. Radiation Biol. Vol. Vol: 4
Country of Publication:
Country unknown/Code not available
Language:
English

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