Adenylyl Cyclase: Determination of Adenylyl Cyclase Activity:
R.A. Johnson and Y. Salomon, Assay of Adenylyl Cyclase Catalytic Activity.
Y. Salomon, Cellular Responsiveness to Hormones and Neurotransmitters: Conversion of [3H]Adenine to [3H]cAMP in Cell Monolayers, Cell Suspensions, and Tissue Slices.
Preparation of Materials Useful in Purification of Components of Hormonally Responsive Adenyl Cyclase Systems:
T.F. Walseth, P.S.T. Yuen, and M.C. Moos, Jr. , Preparation of ~ga-32P-Labeled Nucleoside Triphosphates, Nicotinamide Adenine Dinucleotide, and Cyclic Nucleotides for Use in Determining Adenylyl and Guanylyl Cyclases and Cyclic Nucleotide Phosphodiesterases.
T. Pfeuffer, Synthesis of Forskolin-Agarose Affinity Matrices.
A. Laurenza and K.B. Seamon, High-Affinity Binding Sites for [3H]Forskolin.
Purification of Adenylyl Cyclases:
P. Wang and D.R. Storm, Purification and Characterization of Calmodulin-Sensitive Adenylyl Cyclase from Bovine Brain.
E. Pfeuffer, S. Mollner, and T. Pfeuffer, Purification of Adenylyl Cyclase from Heart and Brain.
W.A. Toscano, Jr., and M.K. Gross, Calmodulin-Mediated Adenylyl Cyclase from Equine Sperm.
G.B. Rosenberg, P. Wang, and D.R. Storm, Isolation of Polyclonal Antibodies against Bovine Brain Calmodulin-Sensitive Adenylyl Cyclases.
S. Mollner and T. Pfeuffer, Characteristics and Use of Monoclonal Antibodies to Various Forms of Adenylyl Cyclase.
T. Braun, Purification of Soluble Form of Adenylyl Cyclase from Testes.
H.R. Masure, M.G. Donovan, and D.R. Storm, Purification and Assay of Cell-Invasive Form of Calmodulin-Sensitive Adenylyl Cyclase from Bordetella pertussis.
S.H. Leppla, Purification and Characterization of Adenylyl Cyclase from Bacillus anthracis.
Guanine Nucleotide-Dependent Regulatory Proteins: Purification and Characterization of G Proteins:
E. Pfeuffer and T. Pfeuffer, Preparation and Application of GTP-Agarose Matrices.
J. Codina, D.J. Carty, L. Birnbaumer, and R. Iyengar, Purification of G Proteins.
K.M. Ferguson and T. Higashijima, Preparation of Guanine Nucleotide-Free G Proteins.
M.P. Graziano, M. Freissmuth, and A.G. Gilman, Purification of Recombinant Gs~ga.
M.E. Linder and A.G. Gilman, Purification of Recombinant Gi~ga and G~ Proteins from Escherichia coli.
S.M. Mumby and A.G. Gilman, Synthetic Peptide Antisera with Determined Specificity for G Protein ~ga or ~gb Subunits.
R.A. Kahn, Quantitation and Purification of ADP-Ribosylation Factor.
J. Moss, S.-C. Tsai, S.R. Price, D.A. Bobak, and M. Vaughan, Soluble Guanine Nucleotide-Dependent ADP-Ribosylation Factors in Activation of Adenylyl Cyclase by Choleragen.
Labeling and Quantitating of G Proteins:
G.S. Kopf and M.J. Woolkalis, ADP-Ribosylation of G Proteins with Pertussis Toxin.
D.M. Gill and M.J. Woolkalis, Cholera Toxin-Catalyzed [32P]ADP-Ribosylation of Proteins.
R.Thomas and T. Pfeuffer, Photoaffinity Labeling of GTP-Binding Proteins.
S. Offermanns, G. Schultz, and W. Rosenthal, Identification of Receptor-Activated G Proteins Using Photoreactive GTP Analog, ~ -32P]GTP Azidoanilide.
D.J. Carty, R.T. Premont, and R. Ivengar, Quantitative Immunoblotting of G-Protein Subunits.
P.J. Casey, I.-H.Pang, and A.G. Gilman, Assay of G-Protein ~gb~gg-Subunit Complex by Catalytic Support of ADP-Ribosylation of Go~ga.
T. Higashijima and K.M. Ferguson, Tryptophan Fluorescence of G Proteins: Analysis of Guanine Nucleotide Binding and Hydrolysis.
R.A. Cerione and E.M. Ross, Reconstitution of Receptors and G Proteins in Phospholipid Vesicles.
Guanylyl Cyclase: Assay of Guanylyl Cyclase:
S.E. Domino, D.J. Tubb, and D.L. Garbers, Assay of Guanylyl Cyclase Catalytic Activity.
Purifcation and Characterization of Guanylyl Cyclase Isozymes:
A. M~adulsch and R. Gerzer, Preparative Polyacrylamide Gel Electrophoresis Apparatus for Purification of Guanylyl Cyclase.
A.A. White and P.J. Lad, Detergent Interactions and Solubilization Techniques for Membrane Guanylyl Cyclase.
C.S. Ramarao and D.L. Garbers, Purification of Membrane Form of Guanylyl Cyclase.
A. M~adulsch and R. Gerzer, Purification of Heme-Containing Soluble Guanylyl Cyclase.
P. Humbert, F. Niroomand, G. Fischer, B. Mayer, D. Koesling, K.-D. Hinsch, G. Schultz, and E. B~adohme, Preparation of Soluble Guanylyl Cyclase from Bovine Lung by Immunoaffinity Chromatography.
S.A. Waldman, D.C. Leitman, and F. Murad, Immunoaffinity Purification of Soluble Guanylyl Cyclase.
S.A. Waldman, D.C. Leitman, and F. Murad, Copurification of Atrial Natriuretic Peptide Receptor and Particulate Guanylyl Cyclase.
T. Inagami, R. Takayanagi, and R.M. Snajdar, Copurification of Atrial Natriuretic Factor Receptors and Guanylyl Cyclase from adrenal Cortex.
S. Singh and D.L. Garbers, Molecular Cloning of Membrane Forms of Guanylyl Cyclase.
M. Potier, C. Huot, C. Koch, P. Hamet, and J.Tremblay, Radiation-Inactivation Analysis of Multidomain Proteins: The Case of Particulate Guanylyl Cyclase.
Regulation of Guanylyl Cyclases:
D.C. Leitman, S.A. Waldman, and F. Murad, Identification of Atrial Natriuretic Peptide Receptors in Cultured Cells.
P. Hamet and J. Tremblay, Evaluating Atrial Natriuretic-Induced cGMP Production by Particulate Guanylyl Cyclase Stimulation in Vitro and in Vivo.
J.K. Bentley, Phosphorylation and Dephosphorylation of Sea Urchin Sperm Cell Guanylyl Cyclase.
J.E. Schultz and S. Klumpp, Calcium-Regulated Guanylyl Cyclases from Paramecium and Tetrahymena. Author Index. Subject Index.
This volume emphasizes methods for the assay, purification, and characterization of adenylyl cyclases, guanine nucleotide-dependent regulatory proteins (G proteins), and guanylyl cyclases.
@introbul:Key Features @bul:* Adenylyl cyclase: determination of activity
- Preparation of materials useful in purification of components of hormonally responsive cyclase systems
- Purification guanine nucleotide-dependent regulatory proteins
- Purification and characterization of g proteins: labeling and quantitating of G proteins
- Reconstitution guanylyl cyclase: assay
- Preparation of materials used for study of the cyclase
Biochemists, endocrinologists, cell and molecular biologists, neuroscientists, analytical and clinical chemists, biomedical researchers, pharmacologists, and physiologists.
- No. of pages:
- © Academic Press 1991
- 4th February 1991
- Academic Press
- eBook ISBN:
- Hardcover ISBN:
@from:Praise for the Volume @qu:"Highly recommended. Methods books are an essential aid to the laboratory worker and this series has a well-deserved international reputation and requires no introduction. As usual, the book is very well presented and the list of contributing authors is extremely impressive. @source:--NEUROSCIENCE @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
School of Medicine Health Sciences Center, University of New York, Stony Brook, U.S.A.
Howard Hughes Medical Institute, Vanderbilt University School of Medicine, Nashville, Tennessee, U.S.A.
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA