Toxicology of Glutathione Transferases

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ISBN: 9780849329838 | 0849329833
Cover: Hardcover
Copyright: 7/27/2006

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The most important enzymes protecting human and other organisms from potentially toxic chemicals, Glutathione S-transferases (GSTs) are central to basic mechanisms such as stress response and physiological functions including protection against lipid peroxidation. This book describes the role of GST in toxicology, focusing on their pharmacologic and physiological roles and their relevance to biological toxicology. It covers structure and function, gene regulation, and these enzymes' involvement in signal transduction. Reflecting current trends in this expanding research area, Toxicology of Glutathione Transferases is the only source that details the methods of GST research.

Chapter 1 Ligandin and Glutathione S-Transferases: Historical Milestones

(10)

Irving Listowsky and Irwin M. Arias

1.1 Early History

(1)

1.2 Ligandin—GST Relationships

(2)

1.3 Intracellular Ligand Binding

(1)

1.4 Major Advances

(1)

1.5 Regulation of GST Gene Expression

(1)

1.6 GSTs and Signaling Pathways

(1)

1.7 Prospects

(1)

References

(6)

Chapter 2 Families of Glutathione Transferases

(16)

Piotr Zimniak and Sharda P Singh

2.1 Introduction and Phylogenetic Distribution

(1)

2.2 Overview: Classification of GSTs

(1)

2.3 Principles of Systematic Nomenclature of Canonical GSTs

(2)

2.4 Brief Description of Individual Classes of GSTs

(6)

2.4.1 MAPEG

(1)

2.4.2 Kappa Class

(1)

2.4.3 Alpha, Mu, and Pi Classes

(1)

2.4.4 Sigma Class

(1)

2.4.5 Theta Class

(1)

2.4.6 Zeta Class

(1)

2.4.7 Omega Class

(1)

2.4.8 Bacterial GSTs: Beta Class

(1)

2.4.9 Insect GSTs: Delta and Epsilon Classes

(1)

2.4.10 Worm GSTs

(1)

2.4.11 Plant GSTs: Phi and Tau Classes

(1)

2.4.12 Fungal GSTs

(1)

Acknowledgment

(1)

References

(6)

Chapter 3 Mammalian Glutathione S-Transferase Genes: Structure and Regulation

(20)

Ian R. Jowsey and John D. Hayes

3.1 Introduction

(1)

3.2 GST Families

(1)

3.3 Catalytic Properties of GSTs

(1)

3.4 Biological Functions of GSTs

(2)

3.5 Regulation of GST Gene Expression

(4)

3.5.1 Identification of the Antioxidant Response Element

(2)

3.5.2 CNC bZIP Transcription Factors Mediate Gene Induction through the ARE

(1)

3.5.3 Nrf2 and Keapl

(1)

3.6 Human GST Genes

(5)

3.6.1 Organization and Chromosomal Localization of Human GST Genes

(1)

3.6.2 Polymorphisms in Human GSTs

(1)

3.6.3 Regulation of Human GST Gene Expression

(2)

3.7 Concluding Remarks

(1)

References

(7)

Chapter 4 Combinatorial Protein Chemistry in Three Dimensions: A Paradigm for the Evolution of Glutathione Transferases with Novel Activities

(24)

Ylva Ivarsson and Bengt Mannervik

4.1 Introduction

(1)

4.2 Chemistry

(2)

4.2.1 The Reactive Sulfur of Glutathione

(1)

4.2.2 Two Major Categories of Detoxication Reactions Catalyzed by GSTs

(1)

4.3 Mechanistic Aspects of Glutathione Conjugation

(4)

4.3.1 Addition Reactions

(2)

4.3.1.1 Epoxides

(1)

4.3.1.2 Alkenes

(2)

4.3.1.3 Organic Isothiocyanates

(1)

4.3.1.4 Quinones

(1)

4.3.2 Nucleophilic Substitutions

(2)

4.3.2.1 Aliphatic Electrophiles

(1)

4.3.2.2 Reductive Substitutions

(1)

4.3.2.3 Aromatic Substitutions

(1)

4.4 Features of the Catalytic Functions of GSTs

(1)

4.4.1 Activation of the Thiol Group of Glutathione

(1)

4.4.2 Activation of the Electrophilic Substrate

(1)

4.5 Rate-Determining Processes

(1)

4.6 Natural Evolution of GSTs

(1)

4.7 The Combinatorial View of GST Structures

(5)

4.7.1 The Glutathione-Binding Module

(1)

4.7.2 A Module for Binding of the Electrophilic Substrate

(1)

4.7.3 Binary Combinations of Protein Subunits

(1)

4.7.4 The Significance of the Quaternary Structure

(2)

4.7.5 Complexes with Other Proteins

(1)

4.8 Proof of Principles and Approaches to Redesign of GSTs by Protein Engineering Based on the Combinatorial Description of Protein Structure

(3)

4.8.1 Determinants of Substrate Selectivities

(1)

4.8.2 Rational Redesign

(1)

4.8.2.1 Primary Structure Alterations

(1)

4.8.2.2 Exchange of Segments of Primary and Secondary Structure

(1)

4.8.3 Stochastic Redesign

(1)

4.8.3.1 Stochastic Recombinations in the Evolution of GSTs with Novel Properties

(1)

4.9 Rate-Limiting Constraints

(1)

4.9.1 What Limits the Efficiency of GST Catalysis?

(1)

4.9.2 Alteration of the Dynamics in the GST Structure

(1)

Acknowledgments

(1)

References

(6)

Chapter 5 Substrates and Reaction Mechanisms of Glutathione Transferases

(32)

Piotr Zimniak

5.1 Introduction

(2)

5.2 Basic Reaction Mechanism of Canonical GSTs

(2)

5.2.1 Binding and Activation of GSH

(2)

5.2.2 Binding of the Electrophilic Substrate

(1)

5.3 Catalytic Activities of GSTs

(11)

5.3.1 Glutathione Transferase Activity

(5)

5.3.2 Glutathione Peroxidase Activity

(1)

5.3.3 Isomerase Activity

(2)

5.3.4 Role in Metabolism of Eicosanoids

(2)

5.3.5 Other Reactions

(1)

5.3.6 Effect of GST Subunit Dimerization on Catalytic Activity

(2)

5.4 Noncatalytic Activities of GSTs

(4)

5.4.1 Ligandin Function

(1)

5.4.2 Modulation of MAP Kinase Signaling via Protein—Protein Interactions

(1)

5.4.3 Other Protein—Protein Interactions

(1)

5.4.4 GSTs as Nitric Oxide Carriers

(1)

5.5 GST Inhibitors

(1)

5.6 Engineered GSTs with New Functions

(2)

Acknowledgment

(1)

References

(11)

Chapter 6 Specificity of Glutathione S-Transferases in the Glutathione Conjugation of Carcinogenic Diol Epoxides

103

(26)

Hui Xiao and Shivendra V. Singh

6.1 Introduction

104

(2)

6.2 Evidence for Protective Effect of GSTs against Activated PAHs

106

(1)

6.3 Specificity of Rodent GSTs in the GSH Conjugation of PAH Diol Epoxides

107

(3)

6.3.1 Specificity of Rat GSTs

107

(1)

6.3.2 Specificity of Murine GSTs

107

(2)

6.3.3 Structural Basis for Catalytic Differences between mGSTA1-1 and mGSTA2-2 toward PAH Diol Epoxides

109

(1)

6.4 Crystal Structures of mGSTAI-1 and mGSTA2-2 in Complex with GSH Conjugate of (+)-anti-BPDE

110

(5)

6.4.1 Active Center and Binding of GSH Conjugate of (+)-anti-BPDE (GSBpd) in mGSTAI-1

110

(2)

6.4.2 Xenobiotic-Induced Conformational Changes in mGSTA1-1

112

(1)

6.4.3 H-Site Comparison of mGSTA1-1 with mGSTA4-4

112

(1)

6.4.4 Role of Arg-216 in mGSTA1-1-Catalyzed GSH Conjugation of (+)-anti-BPDE

113

(1)

6.4.5 GSBpd Binding in the Active Center of mGSTA2-2

113

(2)

6.5 Specificity of Human GSTs toward PAH Diol Epoxides

115

(7)

6.5.1 Kinetic Analysis of Human GSTs toward Diol Epoxides

115

(1)

6.5.2 Structural Basis for Catalytic Differences between hGSTA1-1 and hGSTA2-2 toward (+)-anti-BPDE

116

(2)

6.5.3 Human GSTP1-1 Polymorphism and GSH Conjugation of PAH Diol Epoxides

118

(2)

6.5.4 Crystal Structures of hGSTP1/IA•GSBpd and hGSTP1NA•GSBpd Complexes

120

(1)

6.5.5 Efficacy of hGSTP1-1 Variants against (+)-anti-BPDE-Induced DNA Damage in Cells

121

(1)

6.5.6 Association of hGSTP1 Polymorphism with Cancer Susceptibility

122

(1)

Acknowledgments

122

(1)

References

122

(7)

Chapter 7 GST Polymorphism: Where to Now? Clinical Applications and Functional Analysis

129

(26)

S.L. Holley, A.A. Fryer, W. Carroll, P.R. Hoban, and R.C. Strange

7.1 Introduction

130

(1)

7.2 Structure of the GST Supergene Family

130

(4)

7.3 GST Regulation

134

(1)

7.4 GST Subcellular Localization

134

(1)

7.5 GST Function

135

(4)

7.5.1 GSTs and Xenobiotic Metabolism

135

(1)

7.5.2 GSTs and Cell Cycle Regulation

135

(1)

7.5.3 GSTs, Oxidative Stress, and Apoptosis

136

(1)

7.5.4 GSTs as Mediators of Other Pathways

137

(1)

7.5.5 GSTs and Drug Resistance

137

(1)

7.5.6 GSTP1 in Development

138

(1)

7.6 Polymorphism in GSTs

139

(2)

7.6.1 How Important Are Polymorphisms Within GSTs — Does It All Matter?

140

(1)

7.6.2 GST Knockout Mice

140

(1)

7.6.3 Methylation of GSTs

141

(1)

7.7 Polymorphisms Identified within GSTs

141

(2)

7.7.1 Alpha Class

141

(1)

7.7.2 Mu Class

141

(1)

7.7.3 Theta Class

142

(1)

7.7.4 Pi Class

142

(1)

7.7.5 Zeta Class

142

(1)

7.7.6 Omega Class

142

(1)

7.8 GST Polymorphisms: Clinical Implications

143

(3)

7.8.1 Tobacco-Related Diseases

143

(1)

7.8.2 Oxidative Stress-Related Disorders

144

(1)

7.8.3 Association of GST Genotypes and Disease Severity

145

(1)

7.8.4 Response to Treatment and GST Polymorphisms

145

(1)

7.8.5 Uncharacterized Polymorphisms in GSTs

146

(1)

7.9 Conclusion

146

(1)

References

147

(8)

Chapter 8 Glutathione and Glutathione S-Transferases as Targets for Anticancer Drug Development

155

(24)

Victoria J. Findlay, Danyelle M. Townsend, and Kenneth D. Tew

8.1 Introduction

155

(2)

8.2 S-Glutathionylation

157

(2)

8.3 Glutaredoxin and Sulfiredoxin

159

(1)

8.4 Glutoxim (NOV-002)

160

(2)

8.5 Telintra (TLK199)

162

(4)

8.6 Telcyta (TLK286)

166

(3)

8.7 PABA/NO

169

(2)

8.8 Amifostine (Ethyol)

171

(2)

8.9 Summary

173

(1)

References

174

(5)

Chapter 9 Physiological Substrates of Glutathione S-Transferases

179

(26)

Rajendra Sharma, G.A. Shakeel Ansari, and Yogesh C. Awasthi

9.1 Introduction

179

(1)

9.2 Physiological Substrates of GSTs

180

(3)

9.2.1 Isomerase Activity of GSTs and Steroid Hormone Biosynthesis

181

(2)

9.3 GSTs and Oxidative Metabolism of Arachidonic Acid

183

(5)

9.3.1 Cyclooxygenase Pathway

183

(4)

9.3.2 Lipooxygenase (LOX) Pathway

187

(1)

9.4 GSTs as Antioxidant Enzymes

188

(9)

9.4.1 GSH-Dependent Reduction of Lipid Hydroperoxides

188

(1)

9.4.2 GPx Activity of GSTs

189

(1)

9.4.3 Conjugation Activity of GSTs

190

(1)

9.4.4 Reduction of Membrane PL-OOH by α-Class GSTs

191

(2)

9.4.5 Membrane Association of the α-Class GSTs

193

(1)

9.4.6 Relative Contributions of GSTs and Se-GPxs in Reduction of PL-OOH

194

(1)

9.4.7 Physiological Significance of the GPx Activity of GSTs

195

(2)

9.5 Nonenzymatic Physiological Roles of GSTs

197

(1)

Acknowledgment

198

(1)

References

198

(7)

Chapter 10 Glutathione S-Transferases as Modulators of Signal Transduction

205

(26)

Yusong Yang and Yogesh C. Awasthi

10.1 Introduction

206

(1)

10.2 Lipid Peroxidation and Signaling

206

(4)

10.2.1 Lipid Hydroperoxide–Mediated Signaling

207

(1)

10.2.2 4-HNE and Signaling

208

(1)

10.2.3 Concentration-Dependent Effect of 4-HNE

209

(1)

10.3 GSTs as Determinants of the Intracellular Levels of 4-HNE

210

(2)

10.3.1 GST Isozymes with Substrate Preference for 4-HNE

210

(2)

10.4 Modulation of Signaling by GSTs with GPx Activity

212

(3)

10.4.1 Protection against Stress-Mediated Apoptosis

212

(3)

10.4.2 Inhibition of the Activation of JNK and Caspase 3

215

(1)

10.5 Modulation of 4-HNE--Mediated Signaling by GSTs

215

(9)

10.5.1 Overexpression of 4-HNE–Metabolizing GSTs Promote Proliferation

215

(2)

10.5.2 Inhibition of Differentiation and Apoptosis

217

(1)

10.5.3 Inhibition of the Activation of JNK and Caspases

218

(1)

10.5.4 Accelerated Metabolism of 4-HNE by GSTs Protects against Stress–Induced Apoptosis

219

(1)

10.5.5 Inhibition of GS-HNE Efflux Potentiates Stress-Induced Apoptosis

219

(2)

10.5.6 Depletion of 4-HNE by GSTs Leads to Transformation and Immortalization of Some Adherent Cells

221

(1)

10.5.7 Overexpression of hGSTA4-4 Affects Expression of a Multitude of Genes in HLE B-3 Cells

222

(1)

10.5.8 GSTs Can Modulate Signaling by Interacting with SAPK/JNK

222

(2)

10.6 Future Directions

224

(3)

Acknowledgment

227

(1)

References

227

(4)

Chapter 11 Glutathione-Conjugate Transport and Stress-Response Signaling: Role of RLIP76

231

(26)

Sharad S. Singhal and Sanjay Awasthi

11.1 Introduction

232

(1)

11.2 Transport of GS-E

233

(5)

11.2.1 DNP-SG ATPase

233

(2)

11.2.2 ABC Transporters

235

(1)

11.2.3 Identity of DNP-SG ATPase with a Known GTPase-Activating Protein, RLIP76 (RALBPI)

236

(2)

11.3 The Major Multispecific Transporter of GS-E in Mammalian Tissues

238

(3)

11.4 Pharmacological and Physiological Significance

241

(4)

11.4.1 Drug Resistance

241

(1)

11.4.2 Inflammation

241

(1)

11.4.3 Protection from Heat Shock and Oxidative Stress

242

(1)

11.4.4 Protection from Radiation Toxicity

243

(2)

11.5 A Multifunctional Key Regulatory Protein

245

(1)

11.6 An Integrated Model for Signaling

246

(5)

11.6.1 POB1 Overexpression Induces Apoptosis by Inhibiting RLIP76 Transport Activity

248

(1)

11.6.2 GS-E Transport: Regulation of Receptor-Tyrosine Kinase Signaling and Endocytosis

248

(3)

11.7 Other Activities and Possible Links to GS-E Transport

251

(1)

11.7.1 Roles of Calcium and Cdc2 in Regulating RLIP76 Activity

251

(1)

11.7.2 Mitosis

251

(1)

11.7.3 G-Protein Signaling

251

(1)

Acknowledgment

252

(1)

References

253

(4)

Chapter 12 Glutathione S-Transferases and Oxidative Injury of Cardiovascular Tissues

257

(20)

Yongzhen Yang and Paul J. Boor

12.1 Introduction

257

(2)

12.2 GSH and GST Isozymes in Cardiovascular Tissues

259

(1)

12.3 The Role of GSTs in Doxorubicin Cardiotoxicity

259

(2)

12.3.1 Historical Perspective

259

(1)

12.3.2 Oxidative Stress and Doxorubicin Cardiotoxicity

260

(1)

12.3.3 Doxorubicin Metabolism and Toxicity

260

(1)

12.4 GSH and GSTs during Myocardial and Vascular Injury

261

(2)

12.4.1 The Ischemic Heart

261

(1)

12.4.2 Blood Vessels

262

(1)

12.4.3 Induction of GST by Allylamine

263

(1)

12.5 Studies with Endothelial Cells

263

(3)

12.5.1 The Endothelium and Atherosclerosis

263

(1)

12.5.2 The Role of Specific GST Isozymes

263

(3)

12.6 GSH/GST and Nitrate Tolerance

266

(2)

12.7 GST Polymorphisms and Human Atherosclerosis

268

(2)

12.8 GPx Deficiency and Vascular Disease; Other Factors

270

(1)

12.9 Conclusions

271

(1)

Acknowledgment

272

(1)

References

272

(5)

Chapter 13 Mitochondrial Glutathione S-Transferase Pool in Health and Disease

277

(16)

Haider Raza and Narayan G. Avadhani

13.1 Introduction

277

(2)

13.2 Mitochondrial GSH, ROS, and Respiratory Function

279

(1)

13.2.1 Source and Size of Mitochondrial GSH Pool

279

(1)

13.2.2 The Role of Mitochondrial GSH and ROS in Respiration

280

(1)

13.3 Mitochondrial GSH Pool under Oxidative and Chemical Stress

280

(2)

13.3.1 General Aspects of Mitochondrial GSH

280

(1)

13.3.2 The Role of Mitochondrial GSH in Detoxification of ROS

281

(1)

13.3.3 The Role of Mitochondrial GSH in Nitric Oxide Metabolism

281

(1)

13.4 Multiple Forms of Glutathione S-Transferases in Mitochondria

282

(2)

13.4.1 Mitochondria] GSTK1-1

282

(1)

13.4.2 Other Mitochondria] GST Forms

283

(1)

13.5 Mechanisms of Mitochondrial Import of Cytosolic GSTs

284

(1)

13.5.1 Mechanism of Mitochondrial Targeting of GSTA4-4

284

(1)

13.6 Mitochondria] GSTs in the Pathogenesis of Disease

285

(1)

13.7 Conclusions

286

(1)

Acknowledgments

287

(1)

References

287

(6)

Chapter 14 Activation of Microsomal Glutathione Transferase 1 in Toxicology

293

(28)

Miyuki Shimoji, Yoko Aniya, and Ralf Morgenstern

14.1 Introduction

294

(3)

14.1.1 Microsomal GST (MGST1)

295

(2)

14.2 Conditions Leading to Activation of MGST1

297

(8)

14.2.1 In Vivo Activation

297

(3)

14.2.1.1 Cytochrome P450 (P450) Inducers as Activators of MGST1

297

(1)

14.2.1.2 Activation of MGST1 during Hypoxia

298

(1)

14.2.1.3 Activation of MGST1 by GSH Depletors

299

(1)

14.2.1.4 Lipopolysaccharide (LPS) and D-Galactosamine (GaIN) as Activators of MGST1

299

(1)

14.2.1.5 MGST1 and Diabetes

300

(1)

14.2.2 Effect of Hepatotoxins on MGST1

300

(1)

14.2.2.1 Alpha-Naphtylisothiocyanate (ANIT)

300

(1)

14.2.2.2 Carbon Tetrachloride and 1,2-Dibromo-Ethane

300

(1)

14.2.2.3 Acetaminophen (AAP)

300

(1)

14.2.2.4 Effects of Herbal Extracts on MGST1

301

(1)

14.2.3 In Situ Activation of MGST1: Models of Oxidative Stress and Lipid Peroxidation

301

(1)

14.2.3.1 Ischemia/Reperfusion

301

(1)

14.2.3.2 Organic Hydroperoxide

301

(1)

14.2.4 In Vitro Activation of MGST1

301

(4)

14.2.4.1 N-Ethyl Maleimide

301

(2)

14.2.4.2 Diamide, Cystamine, and Glutathione Disulfide

303

(1)

14.2.4.3 S-Nitrosoglutathione (GSNO) and ONOO-

304

(1)

14.2.4.4 Alpha-Methyldopa and Noradrenaline

304

(1)

14.2.4.5 Acrolein

304

(1)

14.2.4.6 Other Activators

305

(1)

14.3 Activation of MGST1 by Reactive Oxygen Species

305

(3)

14.3.1 Hydrogen Peroxide and Organic Hydroperoxides

305

(1)

14.3.2 MGST1 Activation by an NADPH-Generating System or Xanthine Oxidase (XO)

306

(1)

14.3.3 Antioxidants Including Superoxide Dismutase, Catalase, and Polyphenols

306

(1)

14.3.4 Metal Ions and Ligand Binding

307

(1)

14.3.5 Activation of MGST1 by Limited Proteolysis

307

(1)

14.3.6 Removal of Endogenous Inhibitors

307

(1)

14.4 Miscellaneous Mechanisms

308

(1)

14.5 General Discussion

309

(2)

14.5.1 Induction versus Activation

309

(1)

14.5.2 Different Activation Conditions

309

(1)

14.5.3 Different Enzymatic Activities of MGST1 in Relation to Activation

309

(1)

14.5.4 Mechanism of the Activated Enzyme

310

(1)

14.5.5 Physiological/Toxicological Relevance

310

(1)

Acknowledgments

311

(1)

References

311

(10)

Chapter 15 Glutathione S-Transferase Isozyme Composition of Human Tissues

321

(18)

Shaheen Dhanani and Yogesh C. Awasthi

15.1 Introduction

321

(1)

15.2 Major GST Isozymes of Human Tissues

322

(3)

15.3 Minor GST Isozymes

325

(4)

15.3.1 GST Sigma

326

(1)

15.3.2 GST Theta

326

(1)

15.3.3 GST Omega

327

(1)

15.3.4 GST Zeta

327

(1)

15.3.5 GST Kappa

328

(1)

15.3.6 GST Composition of Cell Lines in Culture

328

(1)

15.3.7 Uncharacterized GSTs

328

(1)

15.3.8 Developmental Patterns of GSTs

329

(1)

15.3.9 Major GST Isozymes of Mice and Rats

329

(1)

15.4 Gender-Related Differences

329

(2)

15.4.1 Gender-Related Difference in Carcinogenicity of Benzo(a)pyrene (B[a]P) in Mice

330

(1)

Acknowledgment

331

(1)

References

331

(8)

Chapter 16 Enzymology of Glutathione S-Transferases: Laboratory Methods

339

(20)

Sharad S. Singhal, Kenneth Drake, Sushma Yadav, Jvotsana Singhal, and Sanjay Awasthi

16.1 Introduction

340

(1)

16.2 GST Activity

341

(6)

16.2.1 Spectrophotometric Methods

341

(4)

16.2.1.1 Transferase Activity

341

(1)

16.2.1.2 1-Chloro-2,4-Dinitro Benzene (CDNB)

342

(1)

16.2.1.3 3,4-Dichloronitrobenzene (DCNB)

343

(1)

16.2.1.4 1,2-Epoxy-3-(P-Nitrophenoxy) Propane (EPNP)

343

(1)

16.2.1.5 Ethacrynic Acids (EA)

343

(1)

16.2.1.6 P-Nitrobenzyl Chloride (NBC)

343

(1)

16.2.1.7 4-Nitropyridine-N-Oxide (NPNO)

344

(1)

16.2.1.8 Bromosulfophthalein (BSP)

344

(1)

16.2.1.9 Trans-4-Phenyl-3-Buten-2-One (tPBO)

344

(1)

16.2.1.10 T-4-Hydroxy-2-Nonenal (4-HNE)

344

(1)

16.2.1.11 Glutathione Peroxidase Activity

344

(1)

16.2.1.12 Lipid Hydroperoxides

345

(1)

16.2.1.13 Nitroglycerin (Glyceryl Trinitrate, GTN)

345

(1)

16.2.2 Thin-Layer Chromatographic Assays

345

(2)

16.2.2.1 Leukotrienes A, Methyl Ester (LTA4ME)

346

(1)

16.2.2.2 Cis-9, 10-Epoxystearic Acid (ESA)

346

(1)

16.2.2.3 Chlorambucil (CLB)

347

(1)

16.3 Purification

347

(6)

16.3.1 GSH-Affinity Purification

347

(1)

16.3.2 Preparation of the GSH-Affinity Resin

348

(1)

16.3.3 Purification of Total GST by GSH-Affinity Chromatography

348

(2)

16.3.3.1 Purification from Human Tissue

348

(1)

16.3.3.2 Cell Lines

349

(1)

16.3.3.3 Bacterially Expressed Recombinant GST

350

(1)

16.3.4 Separation of Individual GST Isoenzymes

350

(2)

16.3.4.1 Liquid Column Electrofocusing

352

(1)

16.3.5 Immuno-Affinity Purification

352

(1)

Acknowledgment

353

(1)

References

353

(6)

Index

359

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Toxicology of Glutathione Transferases

Summary

Table of Contents

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Toxicology of Glutathione Transferases

Summary

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