P. K. Stockman

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The purification of a hybrid glutathione S-transferase (B1 B2) from human liver is described. This enzyme has an isoelectric point of 8.75 and the B1 and B2 subunits are distinguishable immunologically and are ionically distinct. Hybridization experiments demonstrated that B1 B1 and B2 B2 could be resolved by CM-cellulose chromatography and have pI values(More)
Human livers express a variety of cytosolic glutathione S-transferase isoenzymes. The enzymes are subject to a marked polymorphism and the polypeptide basis of the differences in glutathione S-transferase content of individual livers has been investigated by Western blotting, hydroxyapatite HPLC and isoelectric focusing. Collectively, the livers examined(More)
The basic glutathione S-transferases in human liver are composed of at least two immunochemically distinct polypeptides, designated B1 and B2. These subunits exist as homodimers, but can hybridize to form the B1B2 heterodimer [Stockman, Beckett & Hayes (1985) Biochem. J. 227, 457-465]. Although these basic glutathione S-transferases possess similar(More)
The glutathione S-transferases (GST) are a major, multi-gene, group of detoxication proteins. A rapid, two-step purification, that employs S-hexylglutathione affinity chromatography and hydroxyapatite HPLC, is described for the GST isoenzymes in mouse liver. The major hepatic forms comprise Yf(Mr 24,500)-, Ya(Mr 26,000)- and Yb(Mr 27,000)-type subunits. The(More)
Unit of Digestive Oncology, University Hospitals Leuven and KU Leuven, Leuven, Belgium; Biomedical Research Institute, Seoul National University College of Medicine, Seoul, Korea; The Christie NHS Foundation Trust, Manchester; Medical Research Institute, University of Dundee, Dundee; Department of Oncology, Taipei Veterans General Hospital, Taipei, Taiwan;(More)
Sodium dodecyl sulphate polyacrylamide gel electrophoresis This procedure separates poplypeptides according to their size; as it is most commonly used proteins are resolved as a consequence of differences in their rates of migration. SDS/PAGE systems use buffers that contain a detergent, sodium dodecyl sulphate (SDS), which denatures proteins. In a solution(More)
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