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Nitric oxide. Part F, Oxidative and nitrosative stress in redox regulation of cell signaling /
The discovery that nitrogen monoxide or nitric oxide (NO)is a biologically produced free radical has revolutionized our thinking about physiological and pathological processes. This discovery has ignited enormous interest in the scientific community. When generated at low levels, NO is a signaling m...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | , |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Amsterdam ; Boston :
Elsevier/Academic Press,
2008.
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| Colección: | Methods in enzymology ;
v. 440. |
| Temas: | |
| Acceso en línea: | Texto completo Texto completo |
Tabla de Contenidos:
- Cover; Contents; Contributors; Volumes in Series; Section 1: Molecular Methods; Chapter 1: Mass Spectrometric Characterization of Proteins Modified by Nitric Oxide-Derived Species; Abstract; 1. Introduction; 2. Reagents; 3. Preparation of Nitrated BSA; 4. In-Gel Protein Digestion and Mass Spectrometric Analysis; 5. Data Analysis; 6. MALDI-TOF Peptide Mass Fingerprinting; 7. LC-ESI-IT Fragment Fingerprinting upon Collisional Fragmentation; 8. Concluding Remarks; Acknowledgments; References; Chapter 2: Detecting Nitrated Proteins by Proteomic Technologies; Abstract; 1. Introduction; 2. Methods.
- 3. ConclusionsAcknowledgments; References; Chapter 3: Using Tandem Mass Spectrometry to Quantify Site-Specific Chlorination and Nitration of Proteins: Model System Studies with High-Density Lipoprotein Oxidized by Myeloperoxidase; Abstract; 1. Introduction; 2. High-Density Lipoprotein Biology; 3. Advantages of HDL as a Model System; 4. Advantages of LC-ESI-MS/MS When Analyzing Posttranslational Modifications of Proteins; 5. Isolating HDL, ApoA-I, and MPO; 6. Oxidative Reactions; 7. Proteolytic Digestion of Proteins.
- 8. Liquid Chromatography-Electrospray Ionization Mass Spectrometry (LC-ESI-MS and MS/MS)9. A Combination of Tryptic and Glu-C Digests Provides Complete Sequence Coverage of ApoA-I; 10. HOCl or MPO Preferentially Chlorinates Tyrosine 192 in Lipid-Free ApoA-I; 11. Reagent ONOO-and MPO Nitrate All the Tyrosine Residues in Lipid-Free ApoA-I, but Tyrosine 192 Is the Main Target; 12. HOCl Quantitatively Converts All Three Methionine Residues in ApoA-I to Methionine Sulfoxide; 13. HOCl Generates Hydroxytryptophan and Dihydroxytryptophan Residues in ApoA-I.
- 14. Reactive Nitrogen Species Generates Nitrotryptophan Residues in Lipid-Free ApoA-I15. The YXXK Motif Directs ApoA-I Chlorination; 16. Quantitative Analysis of Posttranslational Modifications of Proteins; 17. ApoA-I Oxidation Impairs Cholesterol Transport by the ABCA1 System; 18. Conclusions; Acknowledgments; References; Chapter 4: Influence of Intramolecular Electron Transfer Mechanism in Biological Nitration, Nitrosation, and Oxidation of Redox-Sensitive Amino Acids; Abstract; 1. Introduction; 2. Methods; 3. Results; Acknowledgments; References.
- Chapter 5: Protein Thiol Modification by Peroxynitrite Anion and Nitric Oxide DonorsAbstract; 1. Introduction; 2. Protein Cysteine Oxidation by ONOO-; 3. Methodology to Detect Protein Thiol Modification; 4. Iodoacetamide Labeling of Proteins after Oxidant Treatment; 5. HPLC Separation of Fluorescein-Labeled Peptides; 6. Detection of Interchain Disulfides by Western Blot; 7. Repair of Protein Disulfides by Thioredoxin Reductase and Glutaredoxin Systems; 8. Thioredoxin Reductase Repair of Protein Disulfides; 9. Quantitation of Protein Disulfides by Measuring NADPH Oxidation.