Analysis by limited proteolysis of domain organization and GSH-site arrangement of bacterial glutathione transferase B1-1.

Aceto, A; Dragani, B; Allocati, N; Angelucci, S; Bucciarelli, T; Sacchetta, P; Di Ilio, C; Martini, F

Aceto, A; Dragani, B; Allocati, N; Angelucci, S; Bucciarelli, T; Sacchetta, P; Di Ilio, C; Martini, F.

Affiliation

Aceto A; Institute of Biochemical Sciences, University G. D'Annunzio of Chieti, Italy.

Int J Biochem Cell Biol ; 27(10): 1033-41, 1995 Oct.

Article in En | MEDLINE | ID: mdl-7496993

Subject(s)

Glutathione Transferase/chemistry; Proteus mirabilis/enzymology; Amino Acid Sequence; Binding Sites; Biological Evolution; Chymotrypsin; Circular Dichroism; Dinitrochlorobenzene/metabolism; Dinitrochlorobenzene/pharmacology; Electrophoresis, Polyacrylamide Gel; Glutathione/analogs & derivatives; Glutathione/pharmacology; Glutathione Transferase/metabolism; Molecular Sequence Data; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Protein Structure, Secondary; Sequence Homology, Amino Acid; Structure-Activity Relationship; Trypsin

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Collection: 01-internacional Database: MEDLINE Main subject: Proteus mirabilis / Glutathione Transferase Language: En Journal: Int J Biochem Cell Biol Journal subject: BIOQUIMICA Year: 1995 Type: Article Affiliation country: Italy

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