Overview
- Editors:
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John W. Ludlow
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University of Rochester Cencer Center, Rochester
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Table of contents (25 protocols)
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Front Matter
Pages i-xiii
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- S. Derek Killilea, Qi Cheng, Zhi-Xin Wang
Pages 23-33
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- John H. Connor, Hai Quan, Carey Oliver, Shirish Shenolikar
Pages 41-58
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- Elizabeth Collins, Alistair T. R. Sim
Pages 79-102
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- Veerle Janssens, Christine Van Hoof, Wilfried Merlevede, Jozef Goris
Pages 103-115
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- Patric Turowski, Ned J. C. Lamb
Pages 117-136
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- John W. Ludlow, Deirdre A. Nelson, Nancy A. Krucher
Pages 137-143
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- Monique Beullens, Willy Stalmans, Mathieu Bollen
Pages 145-155
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- Louis Ragolia, Najma Begum
Pages 157-167
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- Margherita Tognarini, Emma Villa-Moruzzi
Pages 169-183
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- Takayasu Kobayashi, Kazuyuki Kusuda, Motoko Ohnishi, Naoki Chida, Shinri Tamura
Pages 185-189
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- Mariam Dohadwala, Norbert Berndt
Pages 191-199
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- Gemma Pujol, Albert Ferrer, Joaquin Ariño
Pages 201-212
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- Susanne Klumpp, Dagmar Selke
Pages 213-218
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- Samuel C. Edwards, Travis B. Van Dyke, Timothy H. Van Dyke, David L. Brautigan
Pages 219-234
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- Matthew K. Robinson, Eric M. Phizicky
Pages 235-242
About this book
A major mechanism by which cells regulate protein function is to place phosphate groups on serine and threonine residues. Though the steady-state level of protein phosphorylation depends on the relative activities of both kinases and phosphatases, a much greater effort has previously gone into the study of the former that the latter . Today, however, there is an increasing appreciation for the role that protein phosphatases play in the dynamic p- cess of protein phosphorylation . To date, there are four major types of protein serine/threonine phosphatase catalytic subunits, designated protein phosphatase type 1, 2A, 2B, and 2C . Each has been identified by the techniques of protein chemistry and enzymology and can be distinguished from one another by their preference for specific substrates as well as their sensitivity to certain acti- tors and inhibitors . Protein Phosphatase Protocols has been assembled in response to the growing interest these enzymes are receiving . The goal of this compilation is to provide a "how-to" experimental guide to aid newcomers as well as s- soned veterans in their research endeavors, thus further contributing towards our ever increasing knowledge of serine/threonine phosphatases . What you have before you contains contributions by many of the current and emerging leaders in the field . To highlight just a few, these chapters c- tain step-by-step information on how to isolate novel phosphatases and re- latory subunits, assay for activity, and generate immunological reagents for both biochemical and biological characterization of these enzymes .
Reviews
"I would highly recommend this volume for anyone wishing to develop or optimize Ser/Thr protein phosphatase assays and/or biochemical procedures in their laboratories."-The Quarterly Review of Biology
Editors and Affiliations
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University of Rochester Cencer Center, Rochester
John W. Ludlow
