Generation, Detection, and Characterization of Oxygen Radicals in Chemistry, Biochemistry, and Intermediate States of Reduction:
C. von Sonntag and H.-P. Schuchmann, Pulse Radiolysis.
M. Saran and W. Bors, Pulse Radiolysis for Investigation of Nitric Oxide-Related Reactions.
M. D'Aquino, C. Bullion, M. Chopra, D. Devi, S. Devi, C. Dunster, G. James, E. Komuro, E. Niki, F. Raza, F. Robertson, J. Sharma, and R. Willson, Sulfhydryl Free Radical Formation by Sonolysis, by Radiolysis, and Thermally: Vitamin A, Curcumin, Muconic Acid, and Related Conjugated Olefins and References.
C. von Sonntag and H.-P. Schuchmann, Suppression of Hydroxyl Radical Reactions in Biological Systems: Considerations Based on Competition Kinetics.
O.I Aruoma, Deoxyribose Assay for Detecting Hydroxyl Radicals.
H. Kaur and B. Halliwell, Detection of Hydroxyl Radicals by Aromatic Hydroxylation.
P.J. Evans and B. Halliwell, Measurement of Iron and Copper in Biological Systems: Blemycin and Copper-Phenanthroline Assays.
L.M. Weiner, Oxygen Radicals Generation and DNA Scission by Anticancer and Synthetic Quinones.
G.M. Rosen, S. Pou, B.E. Britigan, and M.S. Cohen, Spin Trapping of Hydroxyl Radicals in Biological Systems.
R.P. Mason and K.T. Knecht, In Vivo Detection of Radical Adducts by Electron Spin Resonance.
E. Albano, A. Tomasi, and M. Ingelman-Sundberg, Spin Trapping of Alcohol-Derived Radicals in Microsomes and Reconstituted Systemsby Electron Spin Resonance.
M. Tsuchiya, M. Suematsu, and H. Suzuki, In Vivo Visualization of Oxygen Radical-Dependent Photoemission.
J. Fuchs, N. Groth, T. Herrling, and L. Packer, In Vivo Electron Paramagnetic Resonance Imaging of Skin.
A. Mori, X. Wang, and J. Liu, Electron Spin Resonance Assay of Ascorbate-Free Radicals in Vivo.
N. Gotoh and E. Niki, Measurement of Superoxide Reaction by Chemiluminescence.
Isolation, Characterization, and Assay of Enzymes or Substances Involved in Formation or Removal of Oxygen Radicals:
J.D. Morrow and L.J. Roberts, II, Mass Spectrometry of Prostanoids: F2-Isoprostances Produced by NonCyclooxygenase Free Radical-Catalyzed Mechanism.
R. Cueto, G.L. Squadrito, and W.A. Pryor, Quantifying Aldehydes and Distinguishing Aldehydic Product Profiles from Autooxidation and Ozonation of Unsaturated Fatty Acids.
S.P. Wolff, Ferrous Ion Oxidation in Presence of Ferric Ion Indicator Xylenol Orange for Measurement of Hydroperoxides.
C. Giulivi and E. Cadenas, Ferrylmyoglobin Formation: Chemical Reactivity Toward Electron-Donating Compounds.
A. Roveri, M. Maiorino, and F. Ursini, Enzymatic and Immunological Measurements of Soluable and Membrane-Bound Phospholipid-Hydroperoxide Glutathione Peroxidase.
M. Inoue, Targeting Superoxide Dismutase by Gene and Protein Engineering.
O.T.G. Jones and J.T.Hancock, Assays of Plasma and Membrane NADPH Oxidase.
J.S. Beckman, J. Chen, H. Ischiropoulos, and J.P. Crow, Oxidative Chemistry of Peroxynitrite.
M.E. Murphy and E. Noack, Nitric Oxide Assay Using Hemoglobin Method.
J.M. Hevel and M.A.Marletta, Nitric-Oxide Synthase Assays.
U. Firstermann, J.S. Pollock, W.R. Tracey, and M. Nakane, Isoforms of Nitric-Oxide Synthase: Purification and Regulation.
C.J. Lowenstein and S.H Snyder, Purification, Cloning, and Expression of Nitric-Oxide Synthase.
Methods for Assessing Molecular, Cell, and Tissue Damage: Assay and Repair of Oxidative Damage:
G. van Ginkel and A. Sevanian, Lipid Peroxidation-Induced Membrane Structural Alterations.
W. Jessup, R.T. Dean, and J.M. Gebicki, Iodometric Determination of Hydroperoxides in Lipids and Proteins.
F.P. Corongiu and S. Banni, Detection of Conjugated Dienes by Second Derivative Ultraviolet Spectrophotometry.
O. Sergent, P. Cillard, and J. Cillard, Ultraviolet and Infraed Methods for Analysis of Fatty Acyl Esters in Cellular Systems.
S. Chirico, High-Performance Liquid Chromatography-Based Thiobarbituric Acid Tests.
Y. Yamamoto, Chemiluminescence-Based High-Performance Liquid Chromatography Assay of Lipid Hydroperoxides.
T. Miyazawa, K. Fujimoto, T. Suzuki, and K. Yasuda, Determination of Phospholipid Hydroperoxides using Luminol Chemiluminescence-High-Performance Liquid Chromatography.
G.A.S. Ansari and L.L. Smith, Assay of Cholesterol Autoxidation.
H. Shimaski, Fluorescent Lipid Peroxidation Products.
R.L. Levine, J.A. Williams. E.R. Stadtman, and E. Shacter, Carbonyl Assays for Determination of Oxidatively Modified Proteins.
A.Z. Reznick and L. Packer, Oxidative Damage to Proteins: Spectrophotometric Method for Carbonyl Assay.
C. Giulivi and K.J.A. Davies, Dityrosine: A Marker for Oxidatively Modified Proteins and Selective Proteolysis.
K. Uchida and E.E. Stadtman, Quantitation of 4-Hydroxynonenal Protein Adducts.
M.-L. Hu, Measurement of Protein Thiol Groups and Glutathione in Plasma.
J.A. Thomas, Y.-C. Chai, and C.-H. Jung, Protein S-Thiolation and Dethiolation.
E. Kalef and C. Gitler, Purification of Vicinal Dithiol-Containing Proteins by Arsenical-Based Affinity Chromatography.
C. Gitler, M. Mogyoros, and E. Kalef, Labeling of Protein Vicinal Dithiols: Role of Protein-S2 to Protein-(SH)2 Conversion in Metabolic Regulation and Oxidative Stress.
T.P.M. Akerboom and H. Sies, Transport of Glutathione Disulfide and Glutathione S-Conjugates in Hepatocyte Plasma Membrane Vesicles.
H. Puhl, G. Waeg, and H. Esterbauer, Methods to Determine Oxidation of Low Density Lypoproteins.
D. Bonnefont-Rousselot, M. Gardes-Albert, J. Delattre, and C. Ferradini, Quantitative Low Density Lipoprotein Oxidation by Gamma Radiolysis.
B. Arrio, M. Arrio, D. Bonnefont-Rousselot, J.D. Catudioc, and L. Packer, Assaying Low Density Lipoprotein by Laser Light Scattering.
N. Doussett. G.Ferretti, M. Taus. P. Valdiguig, and G. Curatola, Fluorescence Analysis of Lipoprotein Peroxidation.
W. Sattler, D. Mohr, and R. Stocker, Lipoprotein Isolation and Peroxidation: High-Performance Liquid Chromatography Postcolumn Chemiluminescence.
N. Noguchi and E. Niki, Apolipoprotein B Protein Oxidation in Low Density Lipoproteins.
M. Nakano and S. Koga, Luciferin Derivative for Assay of Myeloperoxidase and Dopamine Metabolism.
A.J. Kettle and C.C. Winterbourn, Chlorination Activity of Myeloperosidase.
J. Jahngen-Hodge, A. Taylor, F. Shang, L.L. Huang, and C. Mura, Oxidative Stress to Lens Crystallins.
K.P. Mitton and J.R. Trevithick, High-Performance Liquid Chromatography-Electrochemical Detection of Antioxidantsin Vertebrate Lens: Glutathione, Tocopherol, and Ascorbate.
G. Rothe and G. Valet, Flow Cytometric Assays of Oxidative Burst Activity in Phagocytes.
W. Seeger, D. Walmrath, F. Grimminger, S. Rosseau, H. Schatte, H.-J. Kramer, L. Ermert, and L. Kiss, Acute Respiratory Distress Syndrome: Model Systems using Isolated Perfused Rabbit Lung.
C.S. Lieber and L.M. DeCarli, Animal Models of Chronic Ethanol Toxicity.
W. Drige, H.P. Eck, and S. Mihm, Oxidant-Antioxidant Status in Human Immunodeficiency Virus Infection.
D.K. Das and N. Maulik, Antioxidant Effectiveness in Ischemia-Reperfusion Tissue Injury.
V. Ravindranath, Animal Models and Molecular Markers for Cerebral Ischemia-Reperfusion Injury in Brain.
C.F. Babbs, Histochemical Methods for Localization of Endothelial Superoxide and Hydrogen Peroxide Generation in Perfused Organs.
D.K. Bhuyan and K.C. Bhuyan, Assessment of Oxidative Stress to the Eye in an Animal Model for Cataract. Index.
Since biological tissues are unstable in an oxygen atmosphere, a great deal of effort is expended by organisms to metabolically limit or repair oxidative tissue damage. This volume of Methods in Enzymology and its companion Volume 234 present methods developed to investigate the roles of oxygen radicals and antioxidants in disease.
@introbul:Key Features @bul: Generation, detection, and characterization of oxygen radicals, chemistry, biochemistry, and intermediate states of reductio Isolation, characterization, and assay of enzymes or substrates involved in formation or removal of oxygen radical
- Methods for assessing molecular, cell, and tissue damage; assays and repair of oxidative damage
Biochemists, pharmacologists, physiologists, and cell biologists.
- No. of pages:
- © Academic Press 1994
- 22nd March 1994
- Academic Press
- eBook ISBN:
- Hardcover ISBN:
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California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
Helmut Sies is an Honorary Member of the American Society for Biochemistry and Molecular Biology. He received an Honorary Ph.D. from the University of Buenos Aires, Argentina in 1996. Dr. Sies is a member of the Northrhine-Westphalian Academy of Sciences, Germany, and a Corresponding Member of both the Academy of Sciences of Heidelberg, Germany, and the Academy of Medicine, Buenos Aires, Argentina. He has received many awards and prizes, including the FEBS Anniversary Prize awarded by the Federation of European Biochemical Societies, 1978; the Distinguished Foreign Scholar award, MASUA, 1985; the Silver Medal, Karolinska Institute, Stockholm, 1986; the Ernst Jung Preis fur Medizin, 1988; the Claudius-Galenus-Preis, 1990; and the ISFE-Preis, 1994. Dr. Sies sereves on the editorial board and advisory committee for twelve journals, has edited numerous books, and has published more than 400 original articles and chapters. He received his M.D. at the University of Munich in 1967 and currently serves as Full Professor and Chairman of the Department of Physiological Chemistry at the University of Düsseldorf.
Institut Fur Physiologische Chemie, Germany