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Mitochondrial function. Part A, Mitochondrial electron transport complexes and reactive oxygen species /
The first of two new volumes covering mitochondria, this volume examines modern methods that have been developed to examine mitochondrial electron transport chain complexes, iron-sulfur proteins and reactive oxygen species. The critically acclaimed laboratory standard for forty years, Methods in Enz...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | , |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
San Diego, California :
Academic Press/Elsevier,
�2009.
|
| Edición: | 1. ed. |
| Colección: | Methods in enzymology ;
v. 456. |
| Temas: | |
| Acceso en línea: | Texto completo Texto completo Texto completo |
MARC
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| 245 | 0 | 0 | |a Mitochondrial function. |n Part A, |p Mitochondrial electron transport complexes and reactive oxygen species / |c edited by William S. Allison and Immo E. Scheffler. |
| 250 | |a 1. ed. | ||
| 260 | |a San Diego, California : |b Academic Press/Elsevier, |c �2009. | ||
| 300 | |a 1 online resource (li, 537 pages, 16 unnumbered pages of plates) : |b illustrations | ||
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| 490 | 1 | |a Methods in enzymology, |x 0076-6879 ; |v v. 456 | |
| 504 | |a Includes bibliographical references and index. | ||
| 588 | 0 | |a Print version record. | |
| 520 | |a The first of two new volumes covering mitochondria, this volume examines modern methods that have been developed to examine mitochondrial electron transport chain complexes, iron-sulfur proteins and reactive oxygen species. The critically acclaimed laboratory standard for forty 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. With more than 400 volumes published, each Methods in Enzymology volume presents material that is relevant in today's labs -- truly an essential publication for researchers in all fields of life sciences. The first of two new volumes covering mitochondria, this volume presents modern methods that have been developed to examine mitochondrial electron transport chain complexes, iron-sulfur proteins and reactive oxygen species. These new techniques provide investigators with sensitive, original approaches to the study of disease states associated with mitochondrial malfunction. 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. With more than 400 volumes published, each Methods in Enzymology volume presents material that is relevant in today's labs -- truly an essential publication for researchers in all fields of life sciences. | ||
| 505 | 0 | |a Front Cover ; Methods in Enzymology: Mitochondrial Function, Part A: Mitochondrial Electron Transport Complexes and Reactive Oxygen Species; Copyright Page; Contents; Contributors; Preface; Methods in Enzymology; Chapter 1: Visualizing Functional Flexibility by Three-Dimensional Electron Microscopy: Reconstructing Complex I of the Mitochondrial Respiratory Chain; 1. Introduction; 2. Random Conical Reconstruction; 3. Application of the Techniques to Complex I From Yarrowia Lipolytica; 4. Conclusion; Acknowledgments; References. | |
| 505 | 8 | |a Chapter 2: Correlated Light and Electron Microscopy/Electron Tomography of Mitochondria in Situ 1. Introduction; 2. Light Microscopy; 3. Electron Microscope Tomography; Acknowledgments; References; Chapter 3: Studies of Complex I by Fourier Transform Infrared Spectroscopy; 1. Spectroscopic Studies of Complex I; 2. FTIR Difference Spectroscopy and Its Application to Complex I; 3. Preparation of Rehydrated Layers of Complex I for ATR-FTIR Spectroscopy; 4. Analysis of Rehydrated Complex I Layers by Perfusion-Induced ATR-FTIR Difference Spectroscopy. | |
| 505 | 8 | |a 5. Analysis of Rehydrated Complex I Layers by Electrochemically-Induced ATR-FTIR Difference Spectroscopy; 6. Model Compounds and Strategies for Interpretation; 7. Example IR Difference Spectra of Complex I; Acknowledgments; References; Chapter 4: Electron Transfer in Respiratory Complexes Resolved by an Ultra-Fast Freeze-Quench Approach; 1. Introduction; 2. Ultra-Fast Freeze-Quench Setup; 3. Sample Preparation; 4. Calibration of the Freeze-Quench Setup; 5. Application of Freeze-Quench Approach for the Monitoring of Complex I Reduction by NADH; References. | |
| 505 | 8 | |a Chapter 5: Use of Ruthenium Photooxidation Techniques to Study Electron Transfer in the Cytochrome bc1 Complex; 1. Introduction; 2. Design and Synthesis of Ruthenium-Labeled Proteins; 3. Measurement of Interprotein Electron Transfer in a Ruthenium-Labeled Protein; 4. Measurement of Electron Transfer between Ruz-39-Cc and Cytochrome bc1; 5. Measurement of Electron Transfer within the Cytochrome bc1 Complex; Acknowledgments; References; Chapter 6: Mass Spectrometric Characterization of the Thirteen Subunits of Bovine Respiratory Complexes that are Encoded in Mitochondrial DNA; 1. Introduction. | |
| 505 | 8 | |a 2. Analysis of Mitochondrial Membranes for mt-Proteins; 3. Analysis of Respiratory Complexes for mt-Proteins; 4. Mass Spectrometric Analysis of mt-Proteins; 5. Conclusions and Perspectives; References; Chapter 7: Tracing Human Mitochondrial Complex I Assembly by Use of GFP-Tagged Subunits; 1. Introduction; 2. Selection of Complex I Subunit for GFP Labeling; 3. Creation of Inducible Cell Line Expressing AcGFP1-tagged NDUFS3; 4. Tracing AcGFP1-Labeled NDUFS3 on BN-PAGE; Acknowledgments; References. | |
| 650 | 0 | |a Mitochondria. | |
| 650 | 0 | |a Active oxygen. | |
| 650 | 0 | |a Electron transport. | |
| 650 | 2 | |a Free Radicals |x chemistry |0 (DNLM)D005609Q000737 | |
| 650 | 2 | |a Reactive Oxygen Species |0 (DNLM)D017382 | |
| 650 | 2 | |a Mitochondria |x physiology |0 (DNLM)D008928Q000502 | |
| 650 | 2 | |a Mitochondria |x pathology |0 (DNLM)D008928Q000473 | |
| 650 | 2 | |a Mitochondria |0 (DNLM)D008928 | |
| 650 | 2 | |a Electron Transport |0 (DNLM)D004579 | |
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| 650 | 6 | |a Oxyg�ene actif. |0 (CaQQLa)201-0023010 | |
| 650 | 6 | |a �Electrons |x Transport. |0 (CaQQLa)201-0018743 | |
| 650 | 7 | |a SCIENCE |x Life Sciences |x Cell Biology. |2 bisacsh | |
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| 650 | 7 | |a Electron transport |2 fast |0 (OCoLC)fst00906714 | |
| 650 | 7 | |a Mitochondria |2 fast |0 (OCoLC)fst01024016 | |
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| 700 | 1 | |a Allison, William S., |d 1935- |e editor. | |
| 700 | 1 | |a Scheffler, Immo E., |e editor. | |
| 776 | 0 | 8 | |i Print version: |t Mitochondrial function. Part A, Mitochondrial electron transport complexes and reactive oxygen species. |b 1st ed. |d San Diego, California : Elsevier/Academic Press, �2009 |z 9780080877761 |w (OCoLC)319070718 |
| 830 | 0 | |a Methods in enzymology ; |v v. 456. |x 0076-6879 | |
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