Ontology highlight
ABSTRACT:
SUBMITTER: Chee CS
PROVIDER: S-EPMC4032647 | biostudies-literature | 2014
REPOSITORIES: biostudies-literature
TheScientificWorldJournal 20140424
Glutathione transferases (GST) were purified from locally isolated bacteria, Acinetobacter calcoaceticus Y1, by glutathione-affinity chromatography and anion exchange, and their substrate specificities were investigated. SDS-polyacrylamide gel electrophoresis revealed that the purified GST resolved into a single band with a molecular weight (MW) of 23 kDa. 2-dimensional (2-D) gel electrophoresis showed the presence of two isoforms, GST1 (pI 4.5) and GST2 (pI 6.2) with identical MW. GST1 was reac ...[more]