FEBS Lett. 1985 Mar 25;182(2):319-22.

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.

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Glutathione S-transferase (transferase pi) from human placenta is identical or closely related to glutathione S-transferase (transferase rho) from erythrocytes. [Biochim Biophys Acta. 1981]
Glutathione S-transferase (transferase pi) from human placenta is identical or closely related to glutathione S-transferase (transferase rho) from erythrocytes.
Guthenberg C, Mannervik B. Biochim Biophys Acta. 1981 Oct 13; 661(2):255-60.
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Hayes PC, Bouchier IA, Beckett GJ. Gut. 1991 Jul; 32(7):813-8.

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Cited by 13 PubMed Central articles

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