Statement of responsibility: edited by Lester Packer. Part A, Monothiols and dithiols, protein thiols, and thiyl radicals
ISBN: 0121821528, 9780121821524
Includes bibliographical references and index.
xxix, 529 p : ill. ; 24 cm.
Monothiols and dithiols, protein thiols, and thiyl radicals; Monothiols and dithiols, protein thiols, and thiyl radicals.; Biothiols
- A. Meister, Glutathione Metabolism.
- H.F. Gilbert, Thiol/Disulfide Exchange Equilibria and Disulfide Bond Stability.
- Thiyl Radicals
- P. Wardman and C. von Sonntag, Kinetic Factors That Control the Fate of Thiyl Radicals in Cells.
- C. Schineich, Kinetics of Thiol Reactions.
- S.A. Everett and P. Wardman, Perthiols as Antioxidants: Radical-Scavenging and Pro-oxidative Mechanisms.
- S.C. Kundu and R.L. Willson, Thiyl (Sulfhydryl/Thiol) Free Radical Reactions, Vitamins, Beta-Carotene, and Superoxide Dismutase in Oxidative Stress: Design and Interpretation of Enzymatic Studies.
- C.C. Winterbourn and D. Metodiewa, Reaction of Superoxide with Glutathione and Other Thiols.
- L.M. Weiner, Quantitative Determination of Thiol Groups in Low and High Molecular Weight Compounds by Electron Paramagnetic Resonance.
- E. Cadenas, Thiyl Radical Formation during Thiol Oxidation by Ferrylmyoglobin.
- R. Munday, In Vivo Toxicity of Thiols: Relationship to Rate of One-Electron Oxidation by Oxyhemoglobin.
- Chemical Basis of Thiol/Disulfide Measurements
- N.S. Kosower and E.M. Kosower, Diamide: An Oxidant Probe for Thiols.
- E.M. Kosower and N.S. Kosower, Bromobimane Probes for Thiols.
- G.L. Newton and R.C. Fahey, Determination of Biothiols by Bromobimane Labeling and High-Performance Liquid Chromatography.
- R. Singh, G.V. Lamoureux, W.J. Lees, and G.M. Whitesides, Reagents for Rapid Reduction of Disulfide Bonds.
- K. Becker and R.H. Schirmer, 1,3-Bis(2-chloroethyl)-1-nitrosourea as Thiol-Carbamoylating Agent in Biological Systems.
- Monothiols: Measurement in Organs, Cells, Organelles, and Body Fluids
- H. Nohl, K. Stolze, and L.M. Weiner, Noninvasive Measurement of Thiol Levels in Cells and Isolated Organs.
- J.A. Cook and J.B. Mitchell, Measurement of Thiols in Cell Populations from Tumor and Normal Tissue.
- C. Hwang, H.F. Lodish, and A.J. Sinskey, Measurement of Glutathione Redox State in Cytosol and Secretory Pathway of Cultured Cells.
- T.Y. Aw, Assay of Thiols and Disulfides in Intestinal Lymph.
- R. Singh, W.A. Blattler, and A.R. Collinson, Assay for Thiols Based on Reactivation of Papain.
- J. Vita, J. Sastre, M. Asensi,and L. Packer, Assay of Blood Glutathione Oxidation during Physical Exercise.
- P. Reinemer, H.W. Dirr, and R. Huber, X-Ray Structure Methods for Glutathione Binding.
- W. Drige, R. Kinscherf, S. Mihm, D. Galter, S. Roth, H. Gmander, T. Fischbach, and M. Bockstette, Thiols and the Immune System: Effect of N-Acetylcysteine on T Cell System in Human Subjects.
- R. Olivier, Flow Cytometry Technique for Assessing Effects of N-Acetylcysteine on Apoptosis and Cell Viability of Human Immunodeficiency Virus-Infected Lymphocytes.
- C. Gitler and M. Londner, Use of p-Nitrophenyl Disulfide to Measure Reductive Capacity of Intact Cells.
- R.L. Krauth-Siegel, E.M. Jacoby, and R.H. Schirmer, Trypanothione and N1-Glutathionylspermidine: Isolation and Determination.
- D.M. Ziegler and L.L. Poulsen, Estimation of Tissue Cysteamine by Quantitative Thin-Layer Chromatography.
- Dithiols: Alpha-Lipoic Acid
- G.P. Biewenga and A. Bast, Reaction of Lipoic Acid with Ebselen and Hypochlorous Acid.
- D. Han, G.J. Handelman, and L. Packer, Analysis of Reduced and Oxidized Lipoic Acid in Biological Samples by High-Performance Liquid Chromatography.
- T. Kawabata, H.-J. Tritschler, and L. Packer, Reaction of(R,S)-Dihydrolipoic Acid and Homologs with Iron.
- G. Zimmer, L. Mainka, and H. Ulrich, ATP Synthesis and ATPase Activities in Heart Mitoplasts under Influence of R- and S-Enantiomers of Lipoic Acid.
- K. Fujiwara, K. Okamura-Ikeda, and Y. Motokawa, Assay for Protein Lipoylation Reaction.
- Protein Thiols and Sulfides
- R. Wynn and F.M. Richards, Chemical Modification of Protein Thiols: Formation of Mixed Disulfides.
- H. Faulstich and D. Heintz, Reversible Introduction of Thiol Compounds into Proteins by Use of Activated Mixed Disulfides.
- C. Gitler, B. Zarmi, and E. Kalef, Use of Cationic Detergents to Enhance Reactivity of Protein Sulfhydryls.
- R. Wynn and F.M. Richards, Measuring Thiol-Disulfide Exchange Equilibrium Constants for Single Cysteine-Containing Proteins.
- N. Katunuma and E. Kominami, Structure, Properties, Mechanisms, and Assays of Cysteine Protease Inhibitors: Cystatins and E-64 Derivatives.
- R.B. Freedman, H.C. Hawkins, and S.H. McLaughlin, Protein Disulfide-Isomerase.
- S.S. Simons, Jr., and W.B. Pratt, Glucocorticoid Receptor Thiols and Steroid Binding Activity.
- J.A. Thomas, W. Zhao, S. Hendrich, and P. Haddock, Analysis of Cells and Tissues for S-Thiolation of Proteins.
- M. Kussmann and M. Przybylski, Tertiary Structure-Selective Characterization of Protein Dithiol Groups by Phenylarsine Oxide Modification and Mass Spectrometric Peptide Mapping.
- R.N. Perham, Structure and Posttranslational Modification of Lipoyl Domain of 2-Oxo-Acid Dehydrogenase Multienzyme Complexes.
- A. van der Vliet, C.E. Cross, B. Halliwell, and C.A. O'Neill, Plasma Protein Sulfhydryl Oxidation: Effect of Low Molecular Weight Thiols.
- K.L. Maier, A.-G.Lenz, I. Beck-Speier,and U. Costabel, Analysis of Methionine Sulfoxide in Proteins.
- N. Brot, M.A. Rahman, J. Moskovitz, H. Weissbach, J. Strassman, S.O. Yancey, and S.R. Kushner, Escherichia coli Peptide Methionine Sulfoxide Reductase: Cloning, High Expression, andPurification.
- K.M. Noll, Thiol Coenzymes of Methanogens.
- Author Index.
- Subject Index.
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