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1-Chloro-2,4-dinitrobenzene-mediated irreversible inactivation of acidic glutathione S-transferases. Inactivation mechanism--a saturation-type or simple second-order kinetic process?
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- Author(s): Adams PA;Adams PA; Sikakana CN
- Source:
Biochemical pharmacology [Biochem Pharmacol] 1992 Apr 15; Vol. 43 (8), pp. 1757-60.
- Publication Type:
Journal Article
- Language:
English
- Additional Information
- Source:
Publisher: Elsevier Science Country of Publication: England NLM ID: 0101032 Publication Model: Print Cited Medium: Print ISSN: 0006-2952 (Print) Linking ISSN: 00062952 NLM ISO Abbreviation: Biochem Pharmacol Subsets: MEDLINE
- Publication Information:
Publication: Oxford : Elsevier Science
Original Publication: Oxford, New York [etc.] Paragamon Press.
- Subject Terms:
- Abstract:
A critical analysis of the inactivation kinetics exhibited by the acidic human glutathione S-transferase (GST) enzymes is presented. Data on the 1-chloro-2,4-dinitrobenzene (CDNB)-facilitated inactivation of human placental GST pi have been utilized in conjunction with published inactivation data from the literature to answer the following two questions: (a) do the inactivation kinetics deviate significantly from a simple pseudo first-order model? (b) What is the kinetic mechanism of irreversible electrophilic co-substrate-mediated inactivation of human acidic GSTs? Inactivation of human placental GST pi in the presence of 7-aminocephalosporanic acid, a non-electrophilic non-substrate ligand, is characterized and shown to occur via a process analogous to the second mechanism proposed for CDNB inactivation of the enzyme, namely: pH- and [ligand]-independent solvational inactivation.
- Accession Number:
0 (Cephalosporins)
0 (Dinitrochlorobenzene)
9XI67897RG (7-aminocephalosporanic acid)
EC 2.5.1.18 (Glutathione Transferase)
- Publication Date:
Date Created: 19920415 Date Completed: 19920601 Latest Revision: 20201209
- Publication Date:
20221213
- Accession Number:
10.1016/0006-2952(92)90707-p
- Accession Number:
1575771
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