Characterization of glutathione transferase from Xanthomonas campestris.
A single form of glutathione transferase (Xc-GST-4.5) having an isoelectric point at pH 4.5 was resolved from Xanthomonas campestris cytosol by affinity chromatography and isoelectric focusing. HPLC,N-terminal amino acid sequence, and SDS-PAGE analyses indicate that Xc-GST-4.5 is composed of two identical subunits, each with a molecular mass of 22 kDa. As indicated by its substrate specificity, immunological reactivity, and CD spectra, as well as by its N-terminal amino acid sequence, Xc-GST-4.5 appears to be distinct from the other bacterial glutathione transferases, Pm-GST-6.0 and Sm-GST-7.3, previously purified from the cytosolic fraction of Proteus mirabilis and Serratia marcescens. Xc-GST-4.5 also appears to be distinct from the GST so far purified from other sources.
Di Ilio
C
C
Istituti di Scienze Biochimiche, Facoltà di Medicina, Università di Chieti, Italy.
Aceto
A
A
Allocati
N
N
Piccolomini
R
R
Bucciarelli
T
T
Dragani
B
B
Faraone
A
A
Sacchetta
P
P
Petruzzelli
R
R
Federici
G
G
D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017433:Protein Structure, Secondary; D017421:Sequence Analysis; D013379:Substrate Specificity; D016959:Xanthomonas campestris / Q000201:enzymology*
D005982:Glutathione Transferase