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Structural evidence for three different types of glutathione transferase in human tissues
Author(s) -
Ålin Per,
Mannervik Bengt,
Jörnvall Hans
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80324-0
Subject(s) - biochemistry , homology (biology) , residue (chemistry) , glutathione , transferase , glutathione transferase , enzyme , cytosol , peptide sequence , glutathione s transferase , human placenta , amino acid , chemistry , isozyme , biology , placenta , gene , genetics , pregnancy , fetus
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.