Binding of the aflatoxin-glutathione conjugate to mouse glutathione S- transferase A3-3 is saturated at only one ligand per dimer

Journal of Biological Chemistry

Volumn 271, Issue 44, 1996, Pages 27470-27474

  McHugh, Thomas E ^a   Atkins, William M ^a   Rachal, Jagdish K ^a   Kunze, Kent L ^a   Eaton, David L ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; AFLATOXIN; AFLATOXIN B1; DIMER; GLUTATHIONE;

ARTICLE; BINDING AFFINITY; CONJUGATE; DISSOCIATION CONSTANT; ENZYME ACTIVE SITE; EQUILIBRIUM DIALYSIS; FLUORESCENCE; NONHUMAN; PRIORITY JOURNAL; STOICHIOMETRY;

AFLATOXIN B1; ANIMALS; BINDING SITES; CLONING, MOLECULAR; DIMERIZATION; GLUTATHIONE; GLUTATHIONE TRANSFERASE; ISOENZYMES; KINETICS; MICE; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY;

EID: 0029956734     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.44.27470     Document Type: Article

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