Esworthy R S, Doan K, Doroshow J H, Chu F F
Department of Medical Oncology, City of Hope National Medical Center, Duarte, CA 9101.
Gene. 1994 Jul 8;144(2):317-8. doi: 10.1016/0378-1119(94)90400-6.
A human cDNA that encodes a polypeptide that has 94% deduced amino-acid sequence identity to porcine phospholipid hydroperoxide glutathione peroxidase was cloned from a testis library. The sequence shows preservation of the UGA selenocysteine codon, putative active-site Trp and Glu residues and a Tyr residue that is phosphorylated in the porcine protein. The 3'-UTR shows some conservation of sequences implicated in the insertion of selenocysteine at an opal codon in human glutathione peroxidase-1.
