
Protein Phosphorylation
Academic Press
Published on 1. May 1998
Book
Paperback/Softback
596 pages
978-0-12-634490-5 (ISBN)
Description
Assembled in this volume are articles chosen from Methods in Enzymology Volumes 200 and 201 for their contemporary relevance and their usefulness to those new to the study of protein phosphorylation. Major topics include classification of protein kinases and protein phosphatases, assays of protein kinases and protein phosphorylation, purification and cloning of protein kinases and protein phosphatases, and the use of inhibitors of protein kinases and protein phosphatases.
Reviews / Votes
"This is a carefully edited, attractive book that includes the contributions of some 70-plus investigators who are credible authorities in the subject. The protocols presented are time-tested and sufficiently detailed to ensure reproducibility."--Max E. Rafelson, Rush Medical College of Rush University for DOODY'S
More details
Series
Language
English
Place of publication
San Diego
United States
Publishing group
Elsevier Science Publishing Co Inc
Target group
Professional and scholarly
AUDIENCE: Professionals and students in the areas of biochemistry, molecular biology, microbiology, cell biology, endocrinology, biophysics, pharmacology, and physiology.
Dimensions
Height: 229 mm
Width: 152 mm
Weight
1030 gr
ISBN-13
978-0-12-634490-5 (9780126344905)
Copyright in bibliographic data and cover images is held by Nielsen Book Services Limited or by the publishers or by their respective licensors: all rights reserved.
Schweitzer Classification
Persons
Tony Hunter received his Ph.D. in 1969 from the University of Cambridge, England. He joined the Salk Institute in 1975 as an assistant professor and has been a professor since 1982. His current interests are the protein-tyrosine kinases of the Src and growth factor receptor families and the protein-tyrosine phosphatases that remove the phosphates added by protein-tyrosine kinases. He was elected as a Fellow of the Royal Society of London in 1987, a Fellow of the American Academy of Arts and Sciences in 1992, and as an Associate Member of the European Molecular Biology Organization in 1992.
Volume editor
The Salk Institute, La Jolla, California, USA
The Salk Institute, San Diego, California, U.S.A.
Content
Classification of Protein Kinases and Protein Phosphatases:
T. Hunter, Protein Kinase Classification.
S.K. Hanks and A.M. Quinn, Protein Kinase Catalytic Domain Sequence Database: Identification of Conserved Features of Primary Structure and Classification of Family Members.
R.B. Pearson and B.E. Kemp, Protein Kinase Phosphorylation Site Sequences and Consensus Specificity Motifs: Tabulations.
P. Cohen, Classification of Protein-Serine/Threonine Phosphatases: Identification and Quantitation in Cell Extracts.
Assays of Protein Kinases and Protein Phosphorylation:
B.E. Kemp and R.B. Pearson, Design and Use of Peptide Substrates for Protein Kinases.
J.E. Casnellie, Assay of Protein Kinases Using Peptides with Basic Residues for Phosphocellulose Binding.
E. Racker, Use of Synthetic Amino Acid Polymers for Assay of Protein-Tyrosine and Protein-Serine Kinases.
J.F. Hess, R.B. Bourret, and M.I. Simon, Phosphorylation Assays for Proteins of the Two-Component Regulatory System Controlling Chemotaxis in Escherichia coli.
Y.-F. Wei and H.R. Matthews, Identification of Phosphohistidine in Proteins and Purification of Protein-Histidine Kinases.
J.E. Hutchcroft, M. Anostario, Jr., M.L. Harrison, and R.L. Geahlen, Renaturation and Assay of Protein Kinases after Electrophoresis in Sodium Dodecyl Sulfate-Polyacrylamide Gels.
J.E. Ferrell, Jr. and G.S. Martin, Assessing Activities of Blotted Protein Kinases.
M.P. Kamps, Generation and Use of Anti-Phosphotyrosine Antibodies for Immunoblotting.
M.P. Kamps, Determination of Phosphoamino Acid Composition by Acid Hydrolysis of Protein Blotted to Immobilon.
W.J. Boyle, P. van der Geer, and T. Hunter, Phosphopeptide Mapping and Phosphoamino Acid Analysis by Two-Dimensional Separation on Thin-Layer Cellulose Plates.
K. Luo, T.R. Hurley, and B.M. Sefton, Cyanogen Bromide Cleavage and Proteolytic Peptide Mapping of Proteins Immobilized to Membranes.
P. Cohen, B.W. Gibson, and C.F.B. Holmes, Analysis of the in Vivo Phosphorylation States of Proteins by Fast Atom Bombardment Mass Spectrometry and Other Techniques.
H.E Meyer, E. Hoffmann-Posorske, and L.M.G. Heilmeyer, Jr., Determination and Location of Phosphoserine in Proteins and Peptides by Conversion to S-Ethylcysteine.
R.E.H. Wettenhall, R.H. Aebersold, and L.E. Hood, Solid-Phase Sequencing of 32P-Labeled Phosphopeptides at Picomole and Subpicomole Levels.
P.J. Roach and Y. Wang, Identification of Phosphorylation Sites in Peptides Using a Microsequencer.
H.E. Meyer, E. Hoffmann-Posorske, A. Donella-Deana, and H. Korte, Sequence Analysis of Phosphotyrosine-Containing Peptides.
B.M. Sefton, Measurement of Stoichiometry of Protein Phosphorylation by Biosynthetic Labeling.
J.A. Cooper, Estimation of Phosphorylation Stoichiometry by Separation of Phosphorylated Isoforms.
A.J. Czernik, J.-A. Girault, A.C. Nairn, J. Chen, G. Snyder, J. Kebabian, and P. Greengard, Production of Phosphorylaton State-Specific Antibodies.
B.E. Haley, Nucleotide Photoaffinity Labeling of Protein Kinase Subunits.
Purification and Cloning of Protein Kinases and Protein Phosphatases:
S. Ferrari andG. Thomas, Micro- and Macropurification Methods for Protein Kinases.
P. Jeno and G. Thomas, Affinity Purification of Protein Kinases Using Adenosine 5-Triphosphate, Amino Acid, and Peptide Analogs.
S.H. Francis, L. Wolf, and J.D. Corbin, Purification of Type I( and Type I( Isozymes and Proteolyzed Type I( Monomeric Enzyme of cGMP-Dependent Protein Kinase from Bovine Aorta.
K.-P. Huang and F.L. Huang, Purification and Analysis of Protein Kinase C Isozymes.
S. Stabel, D. Schaap, andP.J. Parker, Expression of Protein Kinase C Isotypes Using Baculovirus Vectors.
W.M. Yonemoto, M.L. McGlone, L.W. Slice, and S.S. Taylor, Prokaryotic Expression of Catalytic Subunit of Adenosine Cyclic Monophosphate-Dependent Protein Kinase.
A.F. Wilks, Cloning Members of Protein-Tyrosine Kinase Family Using Polymerase Chain Reaction.
A.R. Frackelton, Jr., M. Posner, B. Kannan, and F. Mermelstein, Generation of Monoclonal Antibodies Against Phosphotyrosine and Their Use for Affinity Purification of Phosphotyrosine-Containing Proteins.
N.K. Tonks, C.D. Diltz, and E.H. Fischer, Purification of Protein-Tyrosine Phosphatases from Human Placenta.
Use of Inhibitors of Protein Kinases and Protein Phosphatases:
B.E. Kemp, R.B.Pearson, and C.M. House, Pseudosubstrate-Based Peptide Inhibitors.
Y.A. Hannun, A.H. Merrill, Jr., and R.M. Bell, Use of Sphingosine as Inhibitor of Protein Kinase C.
H. Hidaka, M. Watanabe, and R. Kobayashi, Properties and Use of H-Series Compounds as Protein Kinase Inhibitors.
T. Tamaoki, Use and Specificity of Staurosporine, UCN-01, and Calphostin C as Protein Kinase Inhibitors.
D.G. Hardie, T.A.J. Haystead, and A.T.R. Sim, Use of Okadaic Acid to Inhibit Protein Phosphatases in Intact Cells.
A. Levitzki, A. Gazit, N. Osherov, I. Posner, and C. Gilon, Inhibition of Protein-Tyrosine Kinases by Tyrphostins.
T. Akiyama and H. Ogawara, Use and Specificity of Genistein as Inhibitor of Protein-Tyrosine Kinases.
Y. Uehara and H. Fukazawa, Use and Selectivity of Herbimycin A as Inhibitor of Protein-Tyrosine Kinases.
K. Umezawa and M. Imoto, Use of Erbstatin as Protein-Tyrosine Kinase Inhibitor.
J.A. Gordon, Use of Vanadate as Protein-Phosphotyrosine Phosphatase Inhibitor.
Subject Index.
T. Hunter, Protein Kinase Classification.
S.K. Hanks and A.M. Quinn, Protein Kinase Catalytic Domain Sequence Database: Identification of Conserved Features of Primary Structure and Classification of Family Members.
R.B. Pearson and B.E. Kemp, Protein Kinase Phosphorylation Site Sequences and Consensus Specificity Motifs: Tabulations.
P. Cohen, Classification of Protein-Serine/Threonine Phosphatases: Identification and Quantitation in Cell Extracts.
Assays of Protein Kinases and Protein Phosphorylation:
B.E. Kemp and R.B. Pearson, Design and Use of Peptide Substrates for Protein Kinases.
J.E. Casnellie, Assay of Protein Kinases Using Peptides with Basic Residues for Phosphocellulose Binding.
E. Racker, Use of Synthetic Amino Acid Polymers for Assay of Protein-Tyrosine and Protein-Serine Kinases.
J.F. Hess, R.B. Bourret, and M.I. Simon, Phosphorylation Assays for Proteins of the Two-Component Regulatory System Controlling Chemotaxis in Escherichia coli.
Y.-F. Wei and H.R. Matthews, Identification of Phosphohistidine in Proteins and Purification of Protein-Histidine Kinases.
J.E. Hutchcroft, M. Anostario, Jr., M.L. Harrison, and R.L. Geahlen, Renaturation and Assay of Protein Kinases after Electrophoresis in Sodium Dodecyl Sulfate-Polyacrylamide Gels.
J.E. Ferrell, Jr. and G.S. Martin, Assessing Activities of Blotted Protein Kinases.
M.P. Kamps, Generation and Use of Anti-Phosphotyrosine Antibodies for Immunoblotting.
M.P. Kamps, Determination of Phosphoamino Acid Composition by Acid Hydrolysis of Protein Blotted to Immobilon.
W.J. Boyle, P. van der Geer, and T. Hunter, Phosphopeptide Mapping and Phosphoamino Acid Analysis by Two-Dimensional Separation on Thin-Layer Cellulose Plates.
K. Luo, T.R. Hurley, and B.M. Sefton, Cyanogen Bromide Cleavage and Proteolytic Peptide Mapping of Proteins Immobilized to Membranes.
P. Cohen, B.W. Gibson, and C.F.B. Holmes, Analysis of the in Vivo Phosphorylation States of Proteins by Fast Atom Bombardment Mass Spectrometry and Other Techniques.
H.E Meyer, E. Hoffmann-Posorske, and L.M.G. Heilmeyer, Jr., Determination and Location of Phosphoserine in Proteins and Peptides by Conversion to S-Ethylcysteine.
R.E.H. Wettenhall, R.H. Aebersold, and L.E. Hood, Solid-Phase Sequencing of 32P-Labeled Phosphopeptides at Picomole and Subpicomole Levels.
P.J. Roach and Y. Wang, Identification of Phosphorylation Sites in Peptides Using a Microsequencer.
H.E. Meyer, E. Hoffmann-Posorske, A. Donella-Deana, and H. Korte, Sequence Analysis of Phosphotyrosine-Containing Peptides.
B.M. Sefton, Measurement of Stoichiometry of Protein Phosphorylation by Biosynthetic Labeling.
J.A. Cooper, Estimation of Phosphorylation Stoichiometry by Separation of Phosphorylated Isoforms.
A.J. Czernik, J.-A. Girault, A.C. Nairn, J. Chen, G. Snyder, J. Kebabian, and P. Greengard, Production of Phosphorylaton State-Specific Antibodies.
B.E. Haley, Nucleotide Photoaffinity Labeling of Protein Kinase Subunits.
Purification and Cloning of Protein Kinases and Protein Phosphatases:
S. Ferrari andG. Thomas, Micro- and Macropurification Methods for Protein Kinases.
P. Jeno and G. Thomas, Affinity Purification of Protein Kinases Using Adenosine 5-Triphosphate, Amino Acid, and Peptide Analogs.
S.H. Francis, L. Wolf, and J.D. Corbin, Purification of Type I( and Type I( Isozymes and Proteolyzed Type I( Monomeric Enzyme of cGMP-Dependent Protein Kinase from Bovine Aorta.
K.-P. Huang and F.L. Huang, Purification and Analysis of Protein Kinase C Isozymes.
S. Stabel, D. Schaap, andP.J. Parker, Expression of Protein Kinase C Isotypes Using Baculovirus Vectors.
W.M. Yonemoto, M.L. McGlone, L.W. Slice, and S.S. Taylor, Prokaryotic Expression of Catalytic Subunit of Adenosine Cyclic Monophosphate-Dependent Protein Kinase.
A.F. Wilks, Cloning Members of Protein-Tyrosine Kinase Family Using Polymerase Chain Reaction.
A.R. Frackelton, Jr., M. Posner, B. Kannan, and F. Mermelstein, Generation of Monoclonal Antibodies Against Phosphotyrosine and Their Use for Affinity Purification of Phosphotyrosine-Containing Proteins.
N.K. Tonks, C.D. Diltz, and E.H. Fischer, Purification of Protein-Tyrosine Phosphatases from Human Placenta.
Use of Inhibitors of Protein Kinases and Protein Phosphatases:
B.E. Kemp, R.B.Pearson, and C.M. House, Pseudosubstrate-Based Peptide Inhibitors.
Y.A. Hannun, A.H. Merrill, Jr., and R.M. Bell, Use of Sphingosine as Inhibitor of Protein Kinase C.
H. Hidaka, M. Watanabe, and R. Kobayashi, Properties and Use of H-Series Compounds as Protein Kinase Inhibitors.
T. Tamaoki, Use and Specificity of Staurosporine, UCN-01, and Calphostin C as Protein Kinase Inhibitors.
D.G. Hardie, T.A.J. Haystead, and A.T.R. Sim, Use of Okadaic Acid to Inhibit Protein Phosphatases in Intact Cells.
A. Levitzki, A. Gazit, N. Osherov, I. Posner, and C. Gilon, Inhibition of Protein-Tyrosine Kinases by Tyrphostins.
T. Akiyama and H. Ogawara, Use and Specificity of Genistein as Inhibitor of Protein-Tyrosine Kinases.
Y. Uehara and H. Fukazawa, Use and Selectivity of Herbimycin A as Inhibitor of Protein-Tyrosine Kinases.
K. Umezawa and M. Imoto, Use of Erbstatin as Protein-Tyrosine Kinase Inhibitor.
J.A. Gordon, Use of Vanadate as Protein-Phosphotyrosine Phosphatase Inhibitor.
Subject Index.