title: Structural evidence for three different types of glutathione transferase in human tissues.
abstract: Cytosolic glutathione transferase was purified from human placenta and human liver. Three different forms of the enzyme were obtained, the acidic (pi), the near-neutral (mu), and the basic (alpha-epsilon) forms; two had free alpha-amino groups (pi, mu) and one had a blocked alpha-amino group (alpha-epsilon). N-terminal sequence analyses and total compositions gave clearly different results for each form, although transferases pi and mu showed 35% sequence homology in the N-terminal regions, with a 1-residue shift in starting position. Consequently, the proteins are concluded to be products of three discrete but related genes.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D005260:Female; D005982:Glutathione Transferase / Q000032:analysis*; D006801:Humans; D007527:Isoenzymes / Q000032:analysis*; D008099:Liver / Q000201:enzymology*; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy
chemical_list: D000596:Amino Acids; D007527:Isoenzymes; D005982:Glutathione Transferase