Spectra of Electronic Paramagnetic Resonance of Irradiated Amino Acids, Peptides, Proteins and Lyophililized Tissues, and the Mechanism of Primary Action of Ionizing Radiation on Biological Objects; SPEKTRY ELEKTRONNOGO PARAMAGNITNOGO REZONANSA OBLUCHENNYKH AMINOKISLOT, PEPTIDOV, BELKOV, I LIOFILIZOVANNYKH TKANEI

Technical Report · Sat Oct 31 04:00:00 EST 1959

OSTI ID:4270322

Blyumenfel'd, L A; Kalmanson, A E

Analysis was made of the spectra of the electronic paramagnetic resonance (EPR) of free radicals appearing as a result of direct action of gamma radiation on biological objects. When amino acids and peptides are irradiated, the free radicals formed produce wide lines of electronic paramagnetic resonance with a superfine structure. Structural interpretation of the electronic paramagnetic resonance spectra observed is possible in a number of cases. The amount of free radicals formed from amino acids and peptides in ionization (i.e., the radical yield of reaction) attains great values. In the majority of native protein preparations (as distinct from amino acids and peptides), the yield of unpaired electrons is very small, being approximately 1000 times less, while electronic paramagnetic resonance spectra are characterized by very narrow single lines without any superfine structure. This testlfies to the fact that in the case of proteins most electrons, knocked out by radiation, re-combine with the holes, while the remaining unpaired electrons are delocalized along the protein molecule. When protein preparations are subjected to preliminary denaturation there appear, after irradiation, doublet signals of electronic paramagnetic resonance with a large yield, typical of isolated hydrogen bonds. The data so obtained are helpful in clarifying the mechanism of primary action of ionizing radiation on protein systems and in disclosing the causes of higher radio resistance of proteins. The results are in agreement with the prevailing conceptions regarding the electronic mechanism of migration of energy in protein systems, which are considered to be admixture semiconductors. (auth)

• Research Organization: U.S.S.R.
• NSA Number: NSA-13-006277
• OSTI ID: 4270322
• Report Number(s): A/CONF.15/P/2079
• Country of Publication: Country unknown/Code not available
• Language: English

Related Subjects

AMINO ACIDS
BIOLOGY AND MEDICINE
CONFIGURATION
ELECTROMAGNETIC FIELDS
ELECTRONS
FREE RADICALS
GAMMA RADIATION
IONIZATION
MAGNETIC RESONANCE
MAGNETISM
MOLECULES
PARAMAGNETISM
PEPTIDES
PROTEINS
QUANTITY RATIO
RADIATION EFFECTS
RADIOBIOLOGY
RADIOSENSITIVITY
RESONANCE
SEMICONDUCTORS
SPECTRA