SECONDARY PROCESSES IN PROTEINS IRRADIATED IN THE DRY STATE

Journal Article · Fri Feb 01 04:00:00 EST 1963 · Radiation Res.

DOI:https://doi.org/10.2307/3571435· OSTI ID:4725797

Henriksen, T; Sanner, T; Pihl, A

The secondary processes occurring in proteins irradiated with x rays in the dry state were followed by electron spin resonance (ESR) spectroscopy. The formation of sulfur radicals was given particular attention. The crystalline proteins were irradiated in vacuum at 77 un. Concent 85% K, and the spectra were recorded at this temperature after stepwise heattreatment at successively increasing temperatures. At 77 un. Concent 85% K uncharacteristic resonance patterns were observed, reflecting the existence of several kinds of ESR center, with no sign of sulfur resonance. On heat treatment the characteristic glycylglycine pattern and/or sulfur pattern found after irradiation of proteins at room temperature appeared. When the samples were heat-treated, the total number of spins first decreased and subsequently increased significantly. The formation of sulfur radicals, which appears at slightly below room temperature, coincides with the increase in the total number of radicals. Quantitative studies on a number of proteins indicated that the extent of sulfur resonance formed at room temperature depends on the ratio cysteine-cystine/glycine. Experiments on modified proteins (thiolated gelatin) demonstrated that more sulfur resonance was formed when the sulfur was present as sulfhydryl groups than when in the disulfide form. The radical yield for proteins was of the same order of magnitude as that for a number of amino acids. Heat-denaturation of proteins in solution did not significantly alter the yields, in contrast to the findings of previous authors. The radical yields at 295 un. Concent 85% K were consistently higher than when the substances were irradiated at 77 un. Concent 85% K and subsequently annealed to 295 un. Concent 85% K. It is suggested that free radicals induced in proteins are in part formed by homolytic rupture of chemical bonds and that unpaired spins are transferred to specific structures partly by intermolecular processes. (auth)

• Research Organization: Norsk Hydro's Inst. for Cancer Research, Montebello, Oslo
• Sponsoring Organization: USDOE
• NSA Number: NSA-17-023160
• OSTI ID: 4725797
• Journal Information: Radiation Res., Journal Name: Radiation Res. Vol. Vol: 18
• Country of Publication: Country unknown/Code not available
• Language: English

Related Subjects

AMINO ACIDS
BIOLOGY AND MEDICINE
CHEMICAL REACTIONS
CRYSTALS
ELECTRONS
FREE RADICALS
GLYCYLGLYCINE
MOLECULES
PROTEINS
QUANTITY RATIO
RADIATION EFFECTS
RESONANCE
SPECTROSCOPY
SPIN
SULFIDES
SULFUR COMPOUNDS
SULFUR HYDRIDES
TEMPERATURE
VACUUM
VARIATIONS
X RADIATION