Sulfhydryl Groups in Radiation Damage

References

• Adelstein S. J. Coenzyme binding by X-irradiated glutamate and lactate dehydrogenase. Biochemistry 1965; 4: 891
   PubMed Web of Science ®Google Scholar
• Armstrong R. C., Charlesby A. The role of tryptophan in the inactivation of deoxyribo-nuclease. Int. J. Radiat. Biol. 1967; 12: 523
   Google Scholar
• Bacq Z. M., Alexander P. Fundamentals of Radiobiology, 2nd Ed. Pergamon Press, London 1961
   Google Scholar
• Barron E. S. G., Dickman S. Studies on the mechanism of action of ionizing radiations. II. Inhibition of sulfhydryl enzymes by alpha, beta, and gamma rays. J. gen. Physiol. 1949; 32: 595
   PubMed Web of Science ®Google Scholar
• Barron E. S. G., Johnson P. Studies on the mechanism of action of ionizing radiations. XI. Inactivation of yeast alcohol dehydrogenase by X-irradiation. Arch. Biochem. 1954; 48: 149
   PubMed Web of Science ®Google Scholar
• Recovery and Repair Mechanisms in Radiobiology. 1967, Brookhaven Symp. of Biology, No. 20
   Google Scholar
• Butler J. A. V., Robins A. B., Rotblat J. The inactivation of α-chymotrypsin by ionizing radiations. Proc. roy. Soc. (Lond.) A 1960; 256: 1
   Web of Science ®Google Scholar
• Chapman A., Sanner T., Pthl A. X-ray inactivation of phosphofructokinase. The relative radiation sensitivity of the catalytic and the al-losteric properties. Biochim. biophys. Acta (Amst.), In press
   Google Scholar
• Damjanovich S., Kleppe K. The reactivity of SH groups in phosphorylase b. Biochim. biophys. Acta (Amst.) 1966; 122: 145
   PubMed Web of Science ®Google Scholar
• Damjanovich S., Sanner T., Pihl A. Preferential protection of the regulatory function of phosphorylase b against X-ray inactivation in solution. Biochim. biophys. Acta (Amst.) 1967; 136: 593
   PubMed Web of Science ®Google Scholar
• Damjanovich S., Sanner T., Pihl A. The role of the allosteric site in the X-ray inactivation of phosphorylase b. Europ. J. Biochem., 1: 34, 196
   Google Scholar
• Dan K. Behavior of sulfhydryl groups in synchronous division. Cell Synchrony, I. L. Cameron, G. M. Padilla. Academic Press, New York 1966; 307
   Google Scholar
• Deakin H., Ord M. G., Stocken L. A. Glucose 6-phosphate dehydrogenase activity and thiol content of thymus nuclei from control and X-irradiated rats. Biochem. J. 1963; 89: 296
   PubMed Web of Science ®Google Scholar
• Dean C. J., Alexander P. Sensitization of radioresistant bacteria to X-rays by iodoacetamide. Nature (Lond.) 1962; 196: 1324
   Web of Science ®Google Scholar
• Eldjarn L., Bremer J. The disulphide-reducing capacity of liver mitochondria. Acta chem. scand. 1963; 17: 59
   Google Scholar
• Friedberg G., Hayden G. A. The effect of gamma radiation on the amino acid content and the enzymatic activity of ATP-creatine phosphotransferase. Arch. Biochem. 1962; 98: 485
   PubMed Web of Science ®Google Scholar
• Gorin G., Quintiliani M., Airee S. K. The inactivation of alcohol dehydrogenase by X-rays and the dose-modifying effect of some added substances. Radiat. Res. 1967; 32: 671
   PubMed Web of Science ®Google Scholar
• Haynes R. H. The interpretation of microbial inactivation and recovery phenomena. Radiat. Res. 1966; 1, Suppl. 6
   Web of Science ®Google Scholar
• Howard-Flanders P. Factors affecting radiation injury to DNA in bacteria and bacteriophage systems. Brookhaven Symp. Biol. 1961; 14: 18
   PubMedGoogle Scholar
• Howard-Flanders P., Boyce R. P. DNA repair and genetic recombination: Studies on mutants of Escherichia coli defective in these processes. Radiat. Res. 1966; 156, Suppl. 6
   Web of Science ®Google Scholar
• Hutchinson F., Ross D. A. Some kinetics of the indirect effect of ionizing radiation on aqueous solutions. Radiat. Res. 1959; 10: 477
   PubMed Web of Science ®Google Scholar
• Jellum E., Eldjarn L. Isolation of SH-con-taining DNA-nucleoproteins by chromatography on organomercurial polysaccharide. Biochim. bio-phys. Acta (Amst.) 1965; 100: 144
   PubMed Web of Science ®Google Scholar
• Johansen I., Howard-Flanders P. Macro-molecular repair and free radical scavenging in the protection of bacteria against X-rays. Radiat. Res. 1965; 24: 184
   PubMed Web of Science ®Google Scholar
• Kleppe K., Damjanovich S. Studies on the SH groups of phosphorylase b. Mechanism of reaction with 5,5′-dithiobis(2-nitrobenzoic acid). Biochemistry, In press
   Google Scholar
• Kleppe K., Sanner T., Pihl A. Preferential inactivation of the allosteric function of aspartate transcarbamylase by X-rays. Biochim. biophys. Acta (Amst.) 1966; 118: 210
   PubMed Web of Science ®Google Scholar
• Lange R., Pihl A. The mechanism of inactivation of SH enzymes by X-rays. Acta chem. scand. 1959; 13: 2126
   Google Scholar
• Lange R., Pihl A. The mechanism of X-ray inactivation of phosphoglyceraldehyde dehydrogenase. Int. J. Radiat. Biol. 1960; 2: 301
   Web of Science ®Google Scholar
• Lange R., Pihl A., Eldjarn L. The inactivation of SH enzymes by X-rays. Int. J. Radiat. Biol. 1959; 1: 73
   Web of Science ®Google Scholar
• Little C., Sanner T., Pihl A. Stimulation of fructose 1,6-diphosphatase by sulfhydryl reagents and interaction between the different enzymic sites in the molecule. Europ. J. Biochem., In press
   Google Scholar
• Little C., Sanner T., Pihl A. X-ray modification of the catalytic and allosteric functions of fructose 1,6-diphosphatase. Biochim. biophys. Acta (Amst.), In press
   Google Scholar
• Madsen N. B. Allosteric properties of phosphorylase b. Biochem. Biophys. Res. Commun. 1964; 15: 390
   Web of Science ®Google Scholar
• Mazia D. Mitosis and the physiology of cell division. The Cell, J. Brachet, A. E. Mirsky. Academic Press, New York 1961; III: 80
   Google Scholar
• Okada S. Inactivation of deoxyribonuclease by X-rays. II. The kinetics of inactivation in aqueous solution. Arch. Biochem. 1957; 67: 102
   PubMed Web of Science ®Google Scholar
• Pihl A., Eldjarn L., Bremer J. On the mode of action of X-ray protective agents. III. The enzymatic reduction of disulfides. J. biol. Chem. 1957; 227: 339
   PubMed Web of Science ®Google Scholar
• Pihl A., Lange R. The interaction of oxidized glutathione, cystamine monosulfoxide, and tetra-thionate with the -SH groups of rabbit muscle D-glyceraldehyde 3-phosphate dehydrogenase. J. biol. Chem. 1962; 237: 1356
   PubMed Web of Science ®Google Scholar
• Pihl A., Sanner T. Protection of sulfhydryl compounds against ionizing radiation. Biochim. biophys. Acta (Amst.) 1963; 78: 537
   PubMed Web of Science ®Google Scholar
• Pihl A., Sanner T. X-ray inactivation of papain in solution. Radiat. Res. 1963; 19: 27
   PubMed Web of Science ®Google Scholar
• Pihl A., Sanner T. Radiation damage on the molecular level and its modification. Progr. Biochem. Pharmacol. 1965; 1: 85
   Google Scholar
• Pontremoli S., Luppis B., Traniello S., Rippa M., Horecker B. L. Fructose diphosphatase from rabbit liver IV. Sulfhydryl groups and their relation to the catalytic activity. Arch. Biochem. 1965; 112: 7
   PubMed Web of Science ®Google Scholar
• Pontremoli S., Traniello S., Enser M., Shapiro S., Horecker B. L. Regulation of fructose diphosphatase activity by disulfide exchange. Proc. nat. Acad. Sci. (Wash.) 1967; 58: 286
   PubMed Web of Science ®Google Scholar
• Quintiliani M., Boccacci M. Factors affecting the in vitro inactivation of aldolase by X-rays. Int. J. Radiat. Biol. 1963; 7: 255
   Web of Science ®Google Scholar
• Robinson J. D. Interaction between protein sulfhydryl groups and lipid double bonds in biological membranes. Nature (Lond.) 1966; 212: 199
   PubMed Web of Science ®Google Scholar
• Romani R. J., Tappel A. L. Anaerobic irradiation of alcohol dehydrogenase, aldolase and ribo-nuclease. Arch. Biochem. 1959; 79: 323
   Web of Science ®Google Scholar
• Sanner T. Reduced pyridine coenzymes as hydrogen donors in repair of radiation damage. Radiat. Res. 1965; 26: 95
   PubMed Web of Science ®Google Scholar
• Sanner T., Pihl A. Studies on the active -SH group of papain and on the mechanism of papain activation by thiols. J. biol. Chem. 1963; 238: 165
   PubMed Web of Science ®Google Scholar
• Sanner T., Pihl A. Significance and mechanism of the indirect effect in bacterial cells. The relative protective effect of added compounds in E. coli B, irradiated in liquid and in frozen suspension. Radiat. Res, In press
   Google Scholar
• Sanner T., Pihl A. Fundamental aspects of enzyme inactivation by ionizing radiation. Enzymological Aspects of the Application of Ionizing Radiation to Food Preservation. IAEA, Vienna 1968, In press
   Google Scholar
• Shapiro B., Eldjarn L. The effects of ionizing radiation on aqueous solutions of cysteamine and cystamine. Radiat. Res. 1955; 3: 255
   PubMed Web of Science ®Google Scholar
• Shapiro B., Kollmann G., Asnen J. Mechanism of the effect of ionizing radiation on sodium uptake by human erythrocytes. Radiat. Res. 1966; 27: 139
   Web of Science ®Google Scholar
• Skrede S. The mechanism of disulphide reduction by mitochondria. Biochem. J. 1968; 108: 693
   PubMed Web of Science ®Google Scholar
• Smith E. L. Active site of papain and covalent ‘high-energy’ bonds of proteins. J. biol. Chem. 1958; 233: 1392
   PubMed Web of Science ®Google Scholar
• Sutherland R. M., Pihl A. Repair of radiation damage to erythrocyte membranes: The reduction of radiation-induced disulfide groups. Radiat. Res. 1968; 34: 300
   PubMed Web of Science ®Google Scholar
• Sutherland R. M., Rothstein A., Weed R. I. Erythrocyte membrane sulfhydryl groups and cation permeability. J. Cell Physiol. 1967; 69: 185
   PubMed Web of Science ®Google Scholar
• Sutherland R. M., Stannard J. N., Weed R. I. Involvement of sulfhydryl groups in radiation damage to the human erythrocyte membrane. Int. J. Radiat. Biol. 1967; 12: 551
   Web of Science ®Google Scholar
• Szybalski W. Molecular events resulting in radiation injury, repair and sensitization of DNA. Radiat. Res 1967; 147, Suppl. 7
   Web of Science ®Google Scholar
• Velick S. F. Coenzyme binding and the thiol groups of glyceraldehyde-3-phosphate dehydrogenase. J. biol. Chem. 1953; 233: 563
   Google Scholar
• Weed R. I., Eber J., Rothstein A. Interaction of mercury with human erythrocytes. J. gen. Physiol. 1962; 45: 395
   PubMed Web of Science ®Google Scholar
• Wilkening V. G., Lal M., Arends M., Armstrong D. A. The cobalt-60γ radiolysis of cysteine in deaerated aqueous solutions at pH values between 5 and 6. J. Phys. Chem. 1968; 72: 185
   PubMed Web of Science ®Google Scholar
• Winstead J. A. The role of sulfhydryl groups in radiation sensitivity and chemical protection in enzymes. Radiat. Res. 1967; 30: 832
   PubMed Web of Science ®Google Scholar