H. Nakasa et al., NUCLEOTIDE-SEQUENCE OF PI CLASS GLUTATHIONE-S-TRANSFERASE IN HUMAN FETAL LIVER, Research communications in molecular pathology and pharmacology, 97(1), 1997, pp. 67-78
The GST Fpi and GST Ppi, pi class glutathione S-transferase (GST), wer
e purified from human fetal livers and placentas, respectively. Both G
ST enzymes were indistinguishable each other in their subunit molecula
r weights, immunochemical properties and substrate specificities. Thre
e clones (pFGP-1, pFGP-2 and pFGP-3) coding for the pi class GST purif
ied from fetal livers were isolated from a human fetal liver cDNA libr
ary. The full-length clone encodes a polypeptide comprising 210 amino
acid including the initiator methionine. All of these cDNA clones were
nearly identical to a human placental cDNA clone, pGpi 2. The pFGP-1
cDNA had only a single base transition accompanied by an amino acid tr
ansition in the coding region, at position 313. The pFGP-2 and pFGP-3
cDNAs were also nearly identical to pGpi 2 cDNA, having only a single
silent C --> T transition in the coding region, at position 555.