Purification and Characterization of DNA Polymerases:
C.M. Joyce and V. Derbyshire, Purification of Escherichia coli DNA Polymerase I and Klenow Fragment.
H. Cai, H. Yu, K. McEntee, and M.F. Goodman, Purification and Properties of DNA Polymerase II from Escherichia coli.
M.G. Cull and C.S. McHenry, Purification of Escherichia coli DNA Polymerase III Holoenzyme.
M.H. Barnes and N.C. Brown, Purification of DNA Polymerase III of Gram-Positive Bacteria.
J.M. Lazaro, L. Blanco, and M. Salas, Purification of Bacteriophage phi29 DNA Polymerase.
P.M.J. Burgers, DNA Polymerases from Saccharomyces cerevisiae. P.G. Mitsis, C.-S. Chiang, and I.R. Lehman, Purification of DNA Polymerase-Primase (DNA Polymerase alpha) and DNA Polymerase delta from Embryos of Drosophila melanogaster.
T.S.-F. Wang, W.C. Copeland, L. Rogge, and Q. Dong, Purification of Mammalian DNA Polymerases: DNA Polymerase alpha.
K.M. Downey and A.G. So, Purification of Mammalian Polymerases: DNA Polymerase delta.
G.S.-J. Chui and S. Linn, Purification of Mammalian Polymerases: DNA Polymerase epsilon.
W.A. Beard and S.H. Wilson, Purification and Domain-Mapping of Mammalian DNA Polymerasebeta.
M.E. Budd and J.L. Campbell, Purification and Enzymatic and Functional Characterization of DNA Polymerase beta-like Enzyme POL4, Expressed during Yeast Meiosis.
S.F.J. Le Grice, C.E. Cameron, and S.J. Benkovic, Purification and Characterization of Human Immunodeficiency Virus Type 1 Reverse Transcriptase.
Structural Analysis of DNA Polymerases:
G.P. Mullen, Solution Structure of DNA Polymerases and DNA Polymerase-Substrate Complexes.
A.D. Clark, Jr., A. Jacobo-Molina, P. Clark, S.H. Hughes, and E. Arnold, Crystallization of Human Immunodeficiency Virus Type 1 Reverse Transcriptase with and without Nucleic Acid Substrates, Inhibitors, and an Antibody Fab Fragment.
Mechanisms of DNA Polymerases:
F. Eckstein and J.B. Thomson, Phosphate Analogs for Study of DNA Polymerases.
N.C. Brown and G.E. Wright, Mechanisms of Inhibition of DNA Polymerases by 2'-Deoxyribonucleoside 5'-Triphosphate Analogs.
K. Bebenek and T.A. Kunkel, Analyzing the Fidelity of DNA Polymerases.
S. Creighton, L.B. Bloom, and M.F. Goodman, Gel Fidelity Assay Measuring Nucleotide Misinsertion, Exonucleolytic Proofreading, and Lesion Bypass Efficiencies.
S.J. Benkovic and C.E. Cameron, Kinetic Analysis of Nucleotide Incorporation and Misincorporation by the Klenow Fragment of Escherichia coli DNA Polymerase I.
R.A. Bambara, P.J. Fay, and L.M. Mallaber, Methods of Analyzing Processivity.
Structure-Function Studies of DNA Polymerases:
L.Blanco and M. Salas, Mutational Analysis of Bateriophage phi29 DNA Polymerase.
W.C. Copeland, Q. Dong, and T.S.-F. Wang, Rationale for Mutagenesis of DNA Polymerase Active Sites: DNA Polymerase alpha.
P. Digard, W.R. Bebrin, and D.M. Coen, Mutational Analysis of DNA Polymerase Substrate Recognition and Subunit Interactions Using Herpes Simplex Virus as Prototype.
L.J. Reha-Krantz, Use of Genetic Analyses to Probe Structure, Function, and Dynamics of Bacteriophage T4 DNA Polymerase.
W.H. Konigsberg, Limited Proteolysis of DNA Polymerases as Probe of Functional Domains.
A. Telesnitsky, S. Blain, and S.P. Goff, Assays for Retroviral Reverse Transcriptase.
V. Derbyshire, J.K. Pinsonneault, and C.M. Joyce, Structure-Function Analysis of the 3'(5'- Exonuclease of DNA Polymerases. Polymerase Accessory Functions, Replication Proteins, Multienzyme Replication Complexes:
S.W. Matson and D.W. Bean, Purification and Biochemical Characterization of Enzymes with DNA Helicase Activity.
L.V. Mendelman, Characterization of DNA Primases.
J. Wittmeyer and T. Formosa, Identifying DNA Replication Complex Components Using Protein Affinity Chromatography.
Z. Kelman, V. Naktinis, and M. O'Donnell, Radiolabeling of Proteins for Biochemical Studies.
J. Turner and M. O'Donnell, Cycling of Escherichia coli DNA Polymerase III from One Sliding Clamp to Another: Model for Lagging Strand.
T.L. Capson, S.J. Benkovic, and N.G. Nossal, PhotochemicalCross-Linking of DNA Replication Proteins at the Primer Terminus.
Z. Debyser, DNA Substrates for Studying Replication Mechanisms: Synthetic Replication Forks.
M.K. Reddy, S.E. Weitzel, S.S. Daube, T.C. Jarvis, and P.H. von Hippel, Using Macromolecular Crowding Agents to Identify Weak Interactions within DNA Replication Complexes.
B. Bartholomew, R.L. Tinker, G.A. Kassavetis, and E.P. Geiduschek, Photochemical Cross-Linking Assay for DNA Tracking by Replication Proteins.
In VitroReplication Systems: Crude and Reconstituted:
R.E. Moses, Permeabilized Cells.
E. Crooke, DNA Synthesis Initiated at oriC: In Vitro Replication Reactions.
K.J. Marians, phiX174-Type Primosomal Proteins: Purification and Assay.
G.S. Brush, T.J. Kelly, and B. Stillman, Identification of Eukaryotic DNA Replication Proteins Using the Simian Virus 40 in Vitro Replication System.
F.E.J. Coenjaerts and P.C. van der Vliet, Adenovirus DNA Replication in a Reconstituted System.
N.G. Nossal, D.M. Hinton, L.J. Hobbs, and P. Spacciapoli, Purification of Bacteriophage T4 DNA Replication Proteins.
DNA Synthesis in Vivo:
G. Mosig and N. Colowick, DNA Replication of Bacteriophage T4 in Vivo.
K. Skarstad, R. Bernander, and E. Boye, Analysis of DNA Replication in Vivo by Flow Cytometry.
K.L. Friedman and B.J. Brewer, Analysis of Replication Intermediates by Two-Dimensional Agarose Gel Electrophoresis.
M.L. DePamphilis, Specific Labeling of Newly Replicated DNA. Author Index. Subject Index.
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 eagerlyawaited, frequently consulted, and praised by researchers and reviewers alike. More than 250 volumes have been published (all of them still in print) and much of the material is relevant even today--truly an essential publication for researchers in all fields of life sciences.
@introbul:Key Features @bul:* Includes descriptions of functional, structural, kinetic, and genetic methods for analyzing major enzymes of DNA replication
- Describes strategies for studying interactions of these proteins during replication
- Provides comprehensive descriptions of uses of prokaryotic and eukaryotic crude in vitro replication systems and reconstitution of such systems from purified proteins
- Includes methods for analyzing DNA replication in vivo
Biochemists, molecular biologists, biophysicists, cell biologists, biomedical researchers, microbiologists, analytical chemists, industrial researchers working on protein products, and geneticists.
- No. of pages:
- © Academic Press 1995
- 11th October 1995
- Academic Press
- eBook ISBN:
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California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
California Institute of Technology, Pasadena, California, U.S.A.