The Journal of General Physiology · 1949 · 196 citations · 6 references
MedicineBiochemistryChemistryRadiation BiophysicsRadiation DosimetryRadiobiologyBiological Effects Of RadiationOxygen EffectRadiation BiologyRadiation ChemistryRadiation SensitivityRadiation ToxicityDissolved OxygenGamma Irradiation EffectsIonizing IrradiationOxidized GlutathionePh DependenceRadiation Chemistry Of Biological MoleculesRadiation OxidationThiol Chemistry
Dilute solutions of sulfhydryl enzymes (phosphoglyceraldehyde dehydrogenase, adenosinetriphosphatase, succinoxidase) showed reduced activity on irradiation by small amounts of x-rays. When the inhibition was partial the enzyme was reactivated on addition of glutathione. When the inhibition was more complete, reactivation was only partial. These observations are interpreted as being due to oxidation of the -SH groups of the protein by the products of water irradiation, the radicals OH and O(2)H, and H(2)O(2) and atomic oxygen. The irreversible inhibition which occurs when the dose of x-rays is increased is attributed to protein denaturation. Inhibition of the non-sulfhydryl enzymes trypsin, catalase, and ribonuclease, which required larger amounts of x-rays, is attributed to protein denaturation. These experiments are further evidence that inhibition of enzymes by ionizing radiations is due to the indirect action of the products of irradiated water rather than to direct ionization of the enzyme through collision with the ionizing radiation.
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<i>Actions of Radiations on Living Cells</i>
D. E. Lea, P. J. Morrison · Physics Today · 1955 · 1.2K citations
Medicine, Cell Biology, Physics +14
Myosin and adenosinetriphosphatase
Kenneth Bailey · Biochemical Journal · 1942 · 312 citations · Full text
Crystalline lactic dehydrogenase from heart muscle
F. B. Straub · Biochemical Journal · 1940 · 156 citations · Full text
The effect of X-rays on the conjugated protein <i>d</i>-amino-acid oxidase
W. M. Dale · Biochemical Journal · 1942 · 115 citations · Full text