Cyclic Nucleotide Cascades: E. Shacte, E.R. Stadtman, S.R. Jurgensen, and P.B. Chock, Role of cAMP in Cyclic Cascade Regulation. S. Swillens, J.-M. Boeynaems, and J.E. Dumont, Theoretical Considerations of the Regulatory Steps in the cAMP Cascade System. T. Ishikawa, K. Matsumoto, and I. Uno, Yeast Mutants Altered in the cAMP Cascade Systems. Assays of Cyclic Nucleotide Levels, Turnover, and Transport: G. Brooker, Improvements in the Automated Radioimmunoassay for cAMP or cGMP. R. Barber and R.W. Butcher, cAMP turnover in Intact Cells. T.F. Walseth, R.M. Graeff, and N.D. Goldberg, Monitoring Cyclic Nucleotide Metabolism in Intact Cells by 180 Labeling. J.D. Corbin, T.W. Gettys, P.F. Blackmore, S.J. Beebe, S.H. Francis, D.B. Glass, J.B. Redmon, V.S. Sheorain, and L.R. Landiss, Purification and Assay of cAMP, cGMP, AND Cyclic Nucleotide Analogs in Cells Treated with Cyclic Nucleotide Analogs. L.L. Brunton and L.E. Heasley, cAMP Export and Its Regulation by Prostaglandin A1. Cyclic Nucleotide Action: Cyclic Nucleotide Action in Mammals: R. Ekanger and S.O. Daloskeland, Use of Antibody-Sepharose Columns to Study Hormonal Activation of cAMP-Dependent Protein Kinase Isozymes. S.A. Livesey and T.J. Martin, Selective Activation of the cAMP-Dependent Protein Kinase Isoenzymes. S.J. Beebe, P.F. Blackmore, T.D. Chrisman, and J.D. Corbin, Use of Synergistic Pairs of Site-Selective cAMP Analogs in Intact Cells. M.C. Mumby and C.W. Scott, cAMP-Dependent Protein Kinase Regulatory Subunit Phosphorylation in Intact Cells. S.O. Daloskeland and D. alOgreid, Ammonium Sulfate Precipitation Assay for the Study of Cyclic Nucleotide Binding to Proteins. R.R. Fiscus and F. Murad, cGMP-Dependent Protein Kinase Activation in Intact Tissues. L.H. Parker Botelho, J.D. Rothermel, R.V. Coombs, and B. Jastorff, cAMP Analog Antagonists of cAMP Action. B.E. Kemp, H.-C. Cheng, and D.A. Walsh, Peptide Inhibitors of cAMP-Dependent Protein Kinase. S.M. Lohmann, P. De Camilli, and U. Walter, Type II cAMP-Dependent Protein Kinase Regulatory Subunit-Binding Proteins. R.A. Mooney, Use of Digitonin-Permeabilized Adipocytes for cAMP Studies. C.E. Cobb and J.D. Corbin, Purification of cAMP-Free and cAMP-Bound Forms of Bovine Heart cAMP-Dependent Protein Kinase Holoenzyme. M. Seville and J.J. Holbrook, Preparation of Regulatory Subunits from Bovine Heart cAMP-Dependent Protein Kinase by a Nondenaturing Method. J.L. Foster and L.M. Hall, Purification of Drosophila cAMP-Dependent Protein Kinase. R.A. Jungmann, M.R. Kuettel, S.P. Squinto, and J. Kwast-Welfeld, Using Immunocolloidal Gold Electron Microscopy to Investigate cAMP-Dependent Protein Kinase Cellular Compartmentalization. C.V. Byus and W.H. Fletcher, Direct Cytochemical Localization of the Free Catalytic Subunit of cAMP-Dependent Protein Kinase. W.H. Fletcher, T.A. Ishida, S.M. Van Patten, and D.A. Walsh, Direct Cytochemical Localization of Regulatory Subunit of cAMP-Dependent Protein Kinase Using Fluoresceinated Catalytic Subunit. Nonmammalian cAMP-Binding Proteins: P. Klein, A. Theibert, and P. Devreotes, Identification and Ligand-Induced Modification of the cAMP Receptor in Dictyostelium. I.T. Weber, Crystallizing Catabolite Gene Activator Protein with cAMP for Structural Analysis. R. Rangel-Aldao, E. Cayama, O. Allende, and F. Triana, Isolation of a Trypanosoma cAMP-Binding Protein Which Is Not a Regulatory Subunit of cAMP-Dependent Protein Kinase. Molecular Genetic Approaches: G.S. McKnight, M.D. Uhler, C.H. Clegg, L.A. Correll, and G.G. Cadd, Application of Molecular Genetic Techniques to the cAMP-Dependent Protein Kinase System. M.O. Showers and R.A. Maurer, Cloning of cDNA for the Catalytic Subunit of cAMP-Dependent Protein Kinase. T. Jahnsen, L. Hedin, V.J. Kidd, T. Schulz, and J.S. Richards, Molecular Cloning of cDNA for a Hormone-Regulated Isoform of the Regulatory Subunit of Type II cAMP-Dependent Protein Kinase from Rat Ovaries. L.D. Saraswat, M. Filutowics, and S. Taylor, Expression and Mutagenesis of the Regulatory Subunit of cAMP-Dependent Protein Kinase in Escherichia coli. Protein Phosphatases. D.L. Brautigan and C.L. Shriner, Methods to Distinguish Various Types of Protein Phosphatase Activity. H.-C. Li, P.F. Simonelli, and L.-J. Huan, Preparation of Protein Phosphatase-Resistant Substrates Using Adeuosine 5'-O-(gg-thio)triphosphate. A. DeGuzman and E.Y.C. Lee, Preparation of Low-Molecular-Weight Forms of Rabbit Muscle Protein in Phosphatase. B.S. Khatra, Purification of Glycogen-Bound High-Molecular-Weight Phosphoprotein Phosphatase from Rabbit Skeletal Muscle. S.J. McNall, L.M. Ballou, E. Villa Moruzzi, and E.H. Fischer, Purification and Characterization of Phosphorylase Phosphatase from Rabbit Skeletal Muscle. P. Cohen, S. Alemany, B.A. Hemmings, T.J. Resink, P. Straolfors, and H.Y. Lim Tung, Protein Phosphatase-1 and Protein Phosphatase-2A from Rabbit Skeletal Muscle. A.A. Stewart and P. Cohen, Protein Phosphatase-2B from Rabbit Skeletal Muscle: A Ca2+-Dependent, Calmodulin-Stimulated Enzyme. C.H. McGowan and P. Cohen, Protein Phosphatase-2C from Rabbit Skeletal Muscle and Liver: A Mg2+-Dependent Enzyme. P. Cohen, J.G. Foulkes, C.F.B. Holmes, G.A. Nimmo, and N.K. Tonks, Inhibitor-1 and Inhibitor-2 from Rabbit Skeletal Muscle. S. Tsuiki, K. Kikuchi, S. Tamura, and A. Hiraga, Purification of a Mg2+-Dependent Protein Phosphatase. M.D. Pato and E. Kerc, Purification of Smooth Muscle Myosin Phosphatase from Turkey Gizzard. General Methods for Studies of Phosphodiesterases: R.L. Kincaid and V.C. Manganiello, Assay of Cyclic Nucleotide Phosphodiesterase Using Radiolabeled and Fluorescent Substrates. D.M. Watterson and T.J. Lukas, Analysis of Phosphodiesterase Reaction Mixtures by High-Performance Liquid Chromatography. S. Ueno and M. Ueck, Cyclic Nucleotide Phosphodiesterase Activity: Histochemical and Cytochemical Methods. J.N. Wells and J.R. Miller, Methylxanthine Inhibitors of Phosphodiesterases. K. Hosono, Acylpeptide Inhibitors of Phosphodiesterase Produced by Bacillus subtilis. V. Manganiello, E. Degerman, and M. Elks, Selective Inhibitors of Specific Phosphodiesterases in Intact Adipocytes. C. Erneux and F. Miot, Cyclic Nucleotide Analogs Used to Study Phosphodiesterase Catalytic and Allosteric Sites. S.J. Beebe, A. Beasley-Leach, and J.D. Corbin, cAMP Analogs Used to Study Low Km Hormone-Sensitive Phosphodiesterase. Methods for Isolation and Studies of Various Phosphodiesterase Isoenzymes. Calmodulin-Stimulated Phophodiesterase: R.S. Hansen, H. Charbonneau, and J.A. Beavo, Purification of Calmodulin-Stimulated Cyclic Nucleotide Phosphodiesterase by Monoclonal Antibody Affinity Chromatography. R.L. Kincaid and M. Vaughan, Purification and Properties of Calmodulin-Activated Cyclic Nucleotide Phosphodiesterase from Mammalian Brain. G. Draetta and C.B. Klee, Purification of Calmodulin-Stimulated Phosphodiesterase by Affinity Chromatography on Calmodulin Fragment 1-77 Linked to Sepharose. R.K. Sharma and J.H. Wang, Isolation of Bovine Brain Calmodulin-Dependent Cyclic Nucleotide Phosphodiesterase Isozymes. J.R. Miller and J.N. Wells, Estimating the Association of Phosphodiesterase with Calmodulin in Intact Cells. R.L. Kincaid, M.L. Billingsley, and M. Vaughan, Preparation of Fluorescent, Cross-Linking, and Biotinylated Calmodulin Derivatives and Their Use in Studies of Calmodulin-Activated Phosphodiesterase and Protein Phosphatase. R.L. Kincaid, Preparation, Characterization, and Properties of Affinity-Purified Antibodies to Calmodulin-Dependent Cyclic Nucleotide Phosphodiesterase and the Protein Phosphatase Calcineurin. H. Hidaka, M. Inagaki, M. Nishikawa, and T. Tanaka, Selective Inhibitors of Calmodulin-Dependent Phosphodiesterase and Other Enzymes. E. Jedlicki, C. Allende, and J.E. Allende, Heat-Sensitive Inhibitor of Calmodulin-Regulated Cyclic Nucleotide Phosphodiesterase. L.J. Van Eldik, Preparation and Use of Iodinated Calmodulin for Studies of Calmodulin-Binding Proteins. K. Purvis and H. Rui, High-Affinity, Calmodulin-Dependent Isoforms of Cyclic Nucleotide Phosphodiesterase in Rat Testis. cGMP-Binding Phosphodiesterases: S.A. Harrison, N. Beier, T.J. Martins, and J.A. Beavo, Isolation and Comparison of Bovine Heart cGMP-Inhibited and cGMP-Stimulated Phosphodiesterases. A.Yamazaki, M. Tatsumi, and M.W. Bitensky, Purification of Rod Outer Segment GTP-Binding Protein Subunits and cGMP Phosphodiesterase by Single-Step Column Chromatography. P. Hamet and J. Tremblay, Platelet cGMP-Binding Phosphodiesterase. S.H. Francis and J.D. Corbin, Purification of cGMP-Binding Protein Phosphodiesterase from Rat Lung. A. Yamazaki, M.W. Bitensky, and J.E. Casnellie, Photoaffinity Labeling of High-Affinity cGMP-Specific Noncatalytic Binding Sites on cGMP Phosphodiesterase of Rod Outer Segments. C. High-Affinity cAMP Phosphodiesterases: E.G. Loten, Liver Low-Km, Hormone-Sensitive Phosphodiesterase. T. Kono, Insulin-Sensitive cAMP Phosphodiesterase in Rat Adipose Tissue. M.D. Houslay, N.J. Pyne, and M.E. Cooper, Isolation and Characterization of Insulin-Stimulated, High-Affinity cAMP Phosphodiesterases from Rat Liver. W.J. Thompson, C.-C. Shen, and S.J. Strada, Preparation of Dog Kidney High-Affinity cAMP Phosphodiesterase. P. de Masancourt and Y. Giudicelli, Brain Low-Km cAMP Phosphodiesterase. Nonmammalian Cyclic Nucleotide Phosphodiesterases: P.G. Grant and R.W. Colman, Purification of cAMP Phosphodiesterase from Platelets. J. Londesborough and K. Suoranta, Zinc-Containing Cyclic Nucleotide Phosphodiesterases from Baker's Yeast. R.L. Davis, Mutational Analysis of Phosphodiesterase in Drosophila. Subject Index. Author Index.
Novel approaches for the study of phosphodiesterases and phosphoprotein phosphatases, as well as those of nonmammalian cyclic nucleotide receptors, are emphasized for the first time in the Methods of Enzymology series. New methods for the study of protein kinases are also presented.
Biochemists, endocrinologists, cell and molecular biologists, analytical and clinical chemists, biomedical researchers, pharmacologists, physiologists.
- No. of pages:
- © Academic Press 1988
- 28th June 1988
- Academic Press
- Hardcover ISBN:
- eBook ISBN:
@from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for biochemists." @source:--JOURNAL OF CHROMATOGRAPHY
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
Howard Hughes Medical Institute, Vanderbilt University School of Medicine, Nashville, Tennessee, U.S.A.
School of Medicine Health Sciences Center, University of New York, Stony Brook, U.S.A.
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