Open AccessPurification and characterization of a novel glutathione transferase from Ochrobactrum anthropi 1
Author(s) -
Favaloro Bartolo,
Melino Sonia,
Petruzzelli Raffaele,
Ilio Carmine,
Rotilio Domenico
Publication year - 1998
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1998.tb12894.x
Subject(s) - glutathione , glutathione s transferase , proteus mirabilis , biochemistry , serratia marcescens , transferase , antiserum , polyacrylamide gel electrophoresis , gel electrophoresis , escherichia coli , biology , molecular mass , chemistry , enzyme , microbiology and biotechnology , antibody , gene , immunology
Glutathione transferase was purified from Ochrobactrum anthropi and its N‐terminal sequence was determined to be MKLYYKVGACSLAPHIILSEAGLPY. The apparent molecular mass of the protein (24 kDa) was determined by SDS‐polyacrylamide gel electrophoresis analysis. The amino acid sequence obtained showed similarities with known bacterial glutathione transferases in the range of 72–64%. Immunoblotting experiments performed with antisera raised against glutathione transferase from O. anthropi did not show cross‐reactivity with two bacterial glutathione transferases belonging to Serratia marcescens and Proteus mirabilis .