Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi.

Ralat, Luis A; Colman, Roberta F

Ralat, Luis A; Colman, Roberta F.

Affiliation

Ralat LA; Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, USA.

Protein Sci ; 12(11): 2575-87, 2003 Nov.

Article in En | MEDLINE | ID: mdl-14573868

Subject(s)

Bridged Bicyclo Compounds/metabolism; Glutathione Transferase/metabolism; Isoenzymes/metabolism; Xenobiotics/metabolism; Animals; Binding Sites; Glutathione S-Transferase pi; Glutathione Transferase/antagonists & inhibitors; Glutathione Transferase/chemistry; Isoenzymes/antagonists & inhibitors; Isoenzymes/chemistry; Kinetics; Ligands; Lung/enzymology; Models, Molecular; Molecular Structure; Protein Conformation; Substrate Specificity; Swine

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bridged Bicyclo Compounds / Xenobiotics / Glutathione Transferase / Isoenzymes Limits: Animals Language: En Journal: Protein Sci Journal subject: BIOQUIMICA Year: 2003 Document type: Article Affiliation country: United States Country of publication: United States

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