Reinvestigation of the role of thiol groups of glyoxalase I purified from yeast (Saccharomyces cerevisiae).
Biochim Biophys Acta
; 1202(1): 157-60, 1993 Sep 03.
Article
en En
| MEDLINE
| ID: mdl-8373819
ABSTRACT
Glyoxalase I has been purified to homogeneity from Saccharomyces cerevisiae and tested with two different thiol reagents, i.e., 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) and 1-chloro-2,4-dinitrobenzene (CDNB). DTNB reacts with four thiol groups per molecule of enzyme and leads to a complete inhibition which is not reversed by addition of the disulfide-reducing agent dithiothreitol. On the other hand, CDNB slightly affects the glyoxalase-I activity and alkylates only one thiol residue/enzyme. In agreement, DTNB reacts with three thiol residues of the CDNB-reacted enzyme and no reactivation is observed after dithiothreitol treatment. The peptide containing the CDNB-reactive thiol group has been isolated and the sequence overlaps the segment 58-63 of the only known primary structure of glyoxalase I from Pseudomonas putida.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
/
Compuestos de Sulfhidrilo
/
Lactoilglutatión Liasa
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1993
Tipo del documento:
Article
País de afiliación:
Italia