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

Article Details

Citation

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Glutathione S-transferase Mu 1P09488Details
Glutathione S-transferase PP09211Details