Structural evidence for three different types of glutathione transferase in human tissues

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Abstract
Cytosolic glutathione transferase was purified from human placenta and human liver. Three different forms of the enzyme were obtained, the acidic (π), the near-neutral (μ), and the basic (α-ϵ) forms; two had free α-amino groups (π,μ) and one had a blocked α-amino group (α-ϵ). N-terminal sequence analyses and total compositions gave clearly different results for each form, although transferases π and μ 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.