Structural evidence for three different types of glutathione transferase in human tissues.
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Alin P, Mannervik B, Jornvall H
Structural evidence for three different types of glutathione transferase in human tissues.
FEBS Lett. 1985 Mar 25;182(2):319-22.
- PubMed ID
- 3979555 [ View in PubMed]
- 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.