UID:
almafu_9958129177202883
Umfang:
1 online resource (389 p.)
Ausgabe:
1st ed.
ISBN:
9786612737985
,
9781282737983
,
1282737988
,
9780123810045
,
0123810043
Serie:
Methods in enzymology, v. 474
Inhalt:
This volume, along with its companion (volume 474), presents methods and protocols dealing with thiol oxidation-reduction reactions and their implications as they relate to cell signaling. The critically acclaimed laboratory standard for 40 years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Over 450 volumes have been published to date, and much of the material is relevant even today--truly an essential publicatio
Anmerkung:
Description based upon print version of record.
,
Front Cover; Methods in Enzymology; Copyright Page; Contents; Contributors; Preface; Volumes in Series; Chapter 1: Engineering of Fluorescent Reporters into Redox Domains to Monitor Electron Transfers; 1. Introduction; 2. The Problem: Low Sensitivity and Improperly Rate-Limited Assays for Redox Functions of Bacterial Peroxiredoxin Systems; 3. The Solution: Engineering of Fluorescent Redox Reporters into the N-Terminal Domain of AhpF and E. coli Grx1; 4. Engineering of Disulfide-Containing Electron Acceptor Domains to Detect Electron Transfers via Fluorescence Changes
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Linkage of Fluorescein to Bacterial AhpC via a Reducible Disulfide Bond5. Materials; 5.1. Solutions; 5.2. Chemical modification agents; 5.3. Proteins; 6. Methods; 6.1. Generation of modified AhpC proteins linked to fluorescein via a disulfide bond; 6.2. Characterization of the fluorescence and activity of the S128W mutant of the NTD S. typhimurium AhpF; 6.3. Fluorescence-based peroxidase activity assays of S. typhimurium AhpC with S128W NTD using stopped-flow analysis; 6.4. Generation and testing of the F6W mutant of E. coli Grx1 as an electron donor to E. coli BCP; 7. Summary; References
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Chapter 2: Blot-Based Detection of Dehydroalanine-Containing Glutathione Peroxidase with the Use of Biotin-Conjugated Cysteam1. Introduction; 2. Oxidative Inactivation of Glutathione Peroxidase and the Conversion of Its Active Site Sec to DHA; 3. Preparation of Biotin-Conjugated Cysteamine; 4. Blot-Based Detection of DHA-GPx1 in RBCs; 5. Effects of Oxidative Stress on the Formation of DHA-GPx1 in RBCs; 6. Concluding Remarks; Acknowledgments; References; Chapter 3: Analysis of the Redox Regulation of Protein Tyrosine Phosphatase Superfamily Members Utilizing a Cysteinyl-Labeling Assay
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1. Introduction2. Active-Site Structure, Catalysis, and Oxidation; 3. Detection Methods; 4. General Principle of the Assay; 5. Solutions; 6. Preparation of the Lysis Buffer; 7. Preparation of the Hypoxic Glove Box; 8. Preparation of Cell Lysates; 9. Cysteinyl-Labeling Assay; 10. Acute Stimulus-Induced Reversible Oxidation of PTPs; 11. Perspectives; 12. Conclusion; References; Chapter 4: Measuring the Redox State of Cellular Peroxiredoxins by Immunoblotting; 1. Introduction; 2. Measurement of Prx Dimerization; 2.1. Principle of the method; 2.2. General method; 2.3. Examples
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3. Measurement of Prx Hyperoxidation3.1. Principle of method; 3.2. General method; 3.3. Examples; 4. Discussion; Acknowledgments; References; Chapter 5: Thiol Redox Transitions by Thioredoxin and Thioredoxin-Binding Protein-2 in Cell Signaling; 1. Functional Regulation of Redox-Sensitive Proteins by Thiol Modification; 1.1. Thioredoxin; 2. Thiol Reduction by the Thioredoxin Redox System; 2.1. Thiol-redox regulation by thioredoxin in kinase-mediated cellular signal transduction
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2.2. Thiol-redox regulation by thioredoxin in nuclear receptors and transcription factors-mediated cellular signal transduction
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English
Weitere Ausg.:
ISBN 9780123810038
Weitere Ausg.:
ISBN 0123810035
Sprache:
Englisch
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