Probing subunit interactions in glutathione S-transferases using affinity labeling

Keyphrases

• Glutathione S-transferase 100%
• Affinity Labeling 100%
• Subunit Interaction 100%
• Binding Site 66%
• Glutathione 66%
• Isozymes 66%
• Xenobiotics 66%
• Cysteine 33%
• Cooperative Interaction 33%
• Estradiol 33%
• Transferases 33%
• Rat Liver 33%
• Active Sites 33%
• Homodimer 33%
• Benzophenone 33%
• Steroid Binding 33%
• Non-substrate 33%
• Natural Ligands 33%
• Photoaffinity Labeling 33%

Pharmacology, Toxicology and Pharmaceutical Science

• Binding Site 100%
• Glutathione 100%
• Transferase 100%
• Isoenzyme 100%
• Xenobiotic Agent 100%
• Cysteine 50%
• Diethylstilbestrol 50%
• Sulfate 50%
• Benzophenone 50%
• Prasterone 50%
• Homodimer 50%
• Glutathione Transferase 50%

Biochemistry, Genetics and Molecular Biology

• Glutathione S-Transferase 100%
• Affinity Label 100%
• Binding Site 66%
• Isozyme 66%
• Cysteine 33%
• Glutathione 33%
• Estradiol 33%
• Active Site 33%
• Sulfate 33%
• Steroid Binding 33%
• Photoaffinity Labeling 33%