Analysis by limited proteolysis of domain organization and GSH-site arrangement of bacterial glutathione transferase B1-1.
Int J Biochem Cell Biol
; 27(10): 1033-41, 1995 Oct.
Article
em En
| MEDLINE
| ID: mdl-7496993
ABSTRACT
Limited proteolysis method has been used to study the structure-function relationship of bacterial glutathione transferase (GSTB1-1). In absence of three-dimensional structural data of prokaryote GST, the results represent the first information concerning the G-site and domains organization of GSTB1-1. The tryptic cleavages occur mainly at the peptide bonds Lys35-Lys36 and Phe43-Leu44, generating two major molecular species of 20-kDa, 3-kDa and traces of 10-kDa. 1-chloro-2,4-dinitrobenzene favoured the proteolysis of the 20-kDa fragment markedly enhancing the production of the 10-kDa peptide by cleaving the chemical bonds Lys87-Ala88 and Arg91-Tyr92. The tryptic cleavage sites of GSTB1-1 was found to be located close to those previously found for the mammalian GSTP1-1 isozyme. It was concluded that despite their low sequence homology (18%), GSTB1-1 and GSTP1-1 displayed similar structural features in their G-site regions and probably a common organization in structural domains.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteus mirabilis
/
Glutationa Transferase
Idioma:
En
Revista:
Int J Biochem Cell Biol
Assunto da revista:
BIOQUIMICA
Ano de publicação:
1995
Tipo de documento:
Article
País de afiliação:
Itália