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Apoptosis - 1st Edition - ISBN: 9780121822231, 9780080496771

Apoptosis, Volume 322

1st Edition

Editors in Chief: John Abelson Melvin Simon
Serial Volume Editor: John Reed
Hardcover ISBN: 9780121822231
eBook ISBN: 9780080496771
Imprint: Academic Press
Published Date: 5th July 2000
Page Count: 569
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Table of Contents

Contributors to Volume 322


Methods in Enzymology

Detection of DNA Cleavage in Apoptotic Cells

Detection of Apoptosis by Annexin V Labeling

Analysis of Apoptotic Cells by Flow and Laser Scanning Cytometry

Quantitative Measurement of Apoptosis Induced by Cytotoxic T Lymphocytes

Apoptotic Nuclease Assays

Analysis of Programmed Cell Death and Apoptosis in Drosophila

Analysis of Programmed Cell Death in the Nematode Caenorhabditis elegans

Caspase Assays

Determination of Caspase Specificities Using a Peptide Combinatorial Library

Criteria for Identifying Authentic Caspase Substrates during Apoptosis

Purification and Use of Granzyme B

Viral Caspase Inhibitors CrmA and p35

Purification and Use of Recombinant Inhibitor of Apoptosis Proteins as Caspase Inhibitors

Monitoring Activity of Caspases and Their Regulators in Yeast Saccharomyces cerevisiae

In Vitro Assays for Caspase-3 Activation and DNA Fragmentation

Cell-Free Apoptosis in Xenopus laevis Egg Extracts

Cytofluorometric Quantitation of Nuclear Apoptosis Induced in a Cell-Free System

Purification of Mitochondria for Apoptosis Assays

Quantitation of Mitochondrial Transmembrane Potential in Cells and in Isolated Mitochondria

Nitrogen Cavitation for Cell Disruption to Obtain Mitochondria from Cultured Cells

Apoptosis-Related Activities Measured with Isolated Mitochondria and Digitonin-Permeabilized Cells

Assays for Cytochrome c Release from Mitochondria during Apoptosis

Purification and Liposomal Reconstitution of Permeability Transition Pore Complex

Monitoring Interactions of Bcl-2 Family Proteins in 96-Well Plate Assays

Analysis of Dimerization of Bcl-2 Family Proteins by Surface Plasmon Resonance

Measuring Pore Formation by Bcl-2 Family Proteins

Assays for Studying Bax-Induced Lethality in the Yeast Saccharomyces cereνisiae

Exploiting the Utility of Yeast in the Context of Programmed Cell Death

Production of Recombinant TRAIL and TRAIL Receptor: Fc Chimeric Proteins

Expression of Lymphotoxins and Their Receptor–Fc Fusion Proteins by Baculovirus

Analysis of the CD95 (APO-1/Fas) Death-Inducing Signaling Complex by High-Resolution Two-Dimensional Gel Electrophoresis

Measurement of Ceramide Levels by the Diacylglycerol Kinase Reaction and by High-Performance Liquid Chromatography–Fluorescence Spectrometry

Measurement of Ceramide Synthase Activity

Measurement of Sphingomyelinase Activity

Assays for JNK and p38 Mitogen-Activated Protein Kinases

Assaying for IκB Kinase Activity

Assays for Akt

Measurement of Cellular Oxidation, Reactive Oxygen Species, and Antioxidant Enzymes during Apoptosis

Volume Regulation and Ion Transport during Apoptosis

Assays for Transglutaminases in Cell Death


Transient Transfection Assay of Cell Death Genes

Sindbis Virus Vector System for Functional Analysis of Apoptosis Regulators

Transduction of Full-Length Tat Fusion Proteins Directly into Mammalian Cells: Analysis of T Cell Receptor Activation-Induced Cell Death

Author Index

Subject Index


Volume 322 of Methods in Enzymology is dedicated to apoptosis. Major topics covered include measuring apoptosis and apoptosis-induced endonucleases, measuring apoptosis in lower organisms, proteases involved in apoptosis and their inhibitors, cell free systems for monitoring steps in apoptosis pathways, mitochondria and apoptosis, bCl-2 family proteins, and studying receptors and signal transduction events implicated in cell survival and cell death. The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.


Biochemists, cell biologists, molecular biologists, microbiologists, and biomedical researchers.


No. of pages:
© Academic Press 2000
5th July 2000
Academic Press
Hardcover ISBN:
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@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

Ratings and Reviews

About the Editors in Chief

John Abelson

Affiliations and Expertise

California Institute of Technology, Division of Biology, Pasadena, U.S.A.

Melvin Simon

Affiliations and Expertise

The Salk Institute, La Jolla, CA, USA

About the Serial Volume Editor

John Reed

Affiliations and Expertise

The Burnham Institute, La Jolla, California, U.S.A.