Identification of a highly reactive sulphydryl group in human placental glutathione transferase by a site-directed fluorescent reagent.
FEBS Lett
; 263(2): 389-91, 1990 Apr 24.
Article
em En
| MEDLINE
| ID: mdl-2335245
ABSTRACT
A fluorescent maleimide derivative, N-(4-anilino-1-naphthyl) maleimide (ANM), a specific probe for thiol groups, reacted with human placental glutathione transferase (GST, EC 2.5.1.18), causing a complete inactivation of the enzyme in a few minutes. The modified enzyme was denatured, alkylated and digested with (L-1-tosylamide-2-phenylethyl chloromethyl ketone)-trypsin. The tryptic digest was analysed by HPLC and a fluorescent peptide was obtained. The sequence of this peptide allowed us, by a comparison with a well known primary structure, to assign the position 47 to the most reactive cysteine of GST enzyme.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Placenta
/
Glutationa Transferase
Tipo de estudo:
Diagnostic_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
1990
Tipo de documento:
Article