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20200326101150.0 |
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180127s2018 mau ob 001 0 eng d |
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|b eng
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|z (OCoLC)1020867179
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|a 572.7
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|a Fe-S Cluster Enzymes.
|n Part B /
|c edited by Sheila S. David.
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| 250 |
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|a First edition.
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| 260 |
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|a Cambridge, Massachusetts :
|b Academic Press,
|c 2018.
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| 300 |
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|a 1 online resource (510 pages)
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| 336 |
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|a text
|b txt
|2 rdacontent
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| 337 |
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|a computer
|b c
|2 rdamedia
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|a online resource
|b cr
|2 rdacarrier
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|a data file
|2 rda
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| 490 |
1 |
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|a Methods in enzymology ;
|v vol. 599
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| 504 |
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|a Includes bibliographical references and indexes.
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|a Print version record.
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|a Front Cover; Fe-S Cluster Enzymes Part B; Copyright; Contents; Contributors; Preface; Chapter One: Iron-Sulfur Clusters in DNA Polymerases and Primases of Eukaryotes; 1. Introduction; 2. Iron-Sulfur Clusters in DNA Polymerases and Primase; 2.1. DNA Polymerases at the Replication Fork; 2.2. Iron-Sulfur Cluster in the Large Subunit of DNA Primase; 2.3. Iron-Sulfur Clusters in B-Family DNA Polymerases; 3. Genetic Evidence for the Important Roles of Iron-Sulfur Clusters in DNA Replication In Vivo; 4. Purification of Eukaryotic B-Family DNA Polymerases; 4.1. Procedure; 4.2. Notes.
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|a 5. Analysis of Iron Content in Protein Samples5.1. Procedure; 5.2. Notes; Acknowledgment; References; Chapter Two: Fe-S Clusters and MutY Base Excision Repair Glycosylases: Purification, Kinetics, and DNA Affinity Measurements; 1. Introduction; 2. Over Expression and Purification of MutY Homologs; 2.1. Considerations for Isolating MutY Homologs; 2.2. Bacteria as an Overexpression Host; 2.3. Purification of E. coli MutY; 2.4. Purification of a Thermophilic Homolog, G. stearothermophilus MutY; 2.5. MBP-MutY for Higher Yields and Solubility; 2.6. Bacterial Expression of M. musculus Mutyh.
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|a 2.7. Eukaryotic Expression System for Production of Homo sapiens MUTYH3. Gel-Based Adenine Glycosylase Assays and Measurements of Kinetic Parameters; 3.1. General Setup and Execution of the Glycosylase Assay; 3.1.1. Radiolabeling the DNA Substrate; 3.1.2. Preparation of a Denaturing Polyacrylamide Gel; 3.1.3. General Assay Setup; 3.1.4. Visualization and Quantitation of Results; 3.1.5. Salt Concentration in Assay Buffer; 3.2. Correcting the Enzyme Concentration for the Percent Active Fraction; 3.3. Determining the Rate of Product Release; 3.4. Assessing the Rate of Glycosidic Bond Cleavage.
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8 |
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|a 4. Gel-Based Assays for Determining MutY-DNA Affinity4.1. General Features and Considerations of Gel-Based Binding Assays With MutY; 4.1.1. Radiolabeling the DNA Substrate; 4.1.2. Preparation of a Nondenaturing Polyacrylamide Gel; 4.1.3. Running an EMSA; 4.1.4. Visualization and Quantitation of Results; 4.2. Measurements of MutY-DNA Dissociation Constants; 4.3. Measurement of DNA Dissociation Rate (koff); 5. Application of Methods to Reveal Roles of the Fe-S Cluster Cofactor in MutY Homologs; Acknowledgments; References.
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|a Chapter Three: Cellular Assays for Studying the Fe-S Cluster Containing Base Excision Repair Glycosylase MUTYH and Homologs1. Introduction; 2. Mutation Suppression Activity Measured in Rifampicin Resistance Assays; 2.1. Overview of the Rifampicin Resistance Assay; 2.2. Transformation and Growth of Cells; 2.3. Determining the Mutation Frequency; 2.3.1. Troubleshooting Tips; 2.4. Case Study: Use of Rifampicin Resistance Assay to Characterize Zn-Linchpin Motif in MUTYH; 3. Analysis of MutY-Mediated Repair of Defined Plasmid Substrates in E. coli.
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|a 3.1. Designing a Plasmid-Based Bacterial Cell Assay.
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| 650 |
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|a Iron-sulfur proteins.
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| 650 |
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2 |
|a Iron-Sulfur Proteins.
|0 (DNLM)D007506
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| 650 |
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7 |
|a SCIENCE
|x Life Sciences
|x Biochemistry.
|2 bisacsh
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| 650 |
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|a Iron-sulfur proteins.
|2 fast
|0 (OCoLC)fst01721284
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| 655 |
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4 |
|a Electronic books.
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| 700 |
1 |
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|a David, Sheila S.,
|e editor.
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| 776 |
0 |
8 |
|i Print version:
|a David, Sheila S.
|t Fe-S Cluster Enzymes Part B.
|d San Diego : Elsevier Science, ©2018
|z 9780128147177
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| 830 |
|
0 |
|a Methods in enzymology ;
|v vol. 599.
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| 856 |
4 |
0 |
|3 ScienceDirect
|u https://www.sciencedirect.com/science/bookseries/00766879/599
|z Full Text via HEAL-Link
|
