Purification and characterization of a novel glutathione transferase from Ochrobactrum anthropi.
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.
Favaloro
B
B
Istituto di Ricerche Farmacologiche Mario Negri, Consorzio Mario Negri Sud, Gennaro Paone Environmental Health Center, Santa Maria Imbaro, Italy. favaloro@cmns.mnegri.it
Melino
S
S
Petruzzelli
R
R
Di Ilio
C
C
Rotilio
D
D
D000918:Antibody Specificity; D001426:Bacterial Proteins / Q000235:genetics / Q000276:immunology; D005982:Glutathione Transferase / Q000235:genetics* / Q000276:immunology / Q000302:isolation & purification*; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology* / Q000235:genetics*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D005982:Glutathione Transferase