Primary and secondary structural analyses of glutathione S-transferase π from human placenta

摘要: Abstract The primary structure of glutathione S-transferase (GST) π from a single human placenta was determined. established by chemical characterization tryptic and cyanogen bromide peptides as well automated sequence analysis the intact enzyme. structural indicated that protein is comprised 209 amino acid residues gave no evidence post-translational modifications. differed deduced determined nucleotide cDNA clone (Kano, T., Sakai, M., Muramatsu, 1987, Cancer Res. 47 , 5626–5630) at position 104 which contained both valine isoleucine whereas identified only this position. These results demonstrated in one individual studied least two GST genes are coexpressed, probably result allelomorphism. Computer assisted consensus evaluation hydrophobic region (residues 155–181) predicted to be either buried transmembrane helical or signal region. significance interpreted relation mode action enzyme especially regard potential involvement histidine active site mechanism. A comparison similarity five known complete structures, π, μ, α, microsomal, all enzymes have evolved divergent evolutionary process after gene duplication, with microsomal representing most form.