Yoshimura S, Suemizu H, Taniguchi Y, Arimori K, Kawabe N, Moriuchi T
Department of Molecular Life Science (Cell Biology), Tokai University School of Medicine, Kanagawa, Japan.
Gene. 1994 Aug 5;145(2):293-7. doi: 10.1016/0378-1119(94)90023-x.
A genomic clone encoding the human plasma glutathione peroxidase (PGPx), a major enzyme in reducing lipid hydroperoxide and hydrogen peroxide in plasma, was isolated and 5618 nucleotides (nt) were determined. The nt sequence data revealed that the PGPx gene is composed of five exons spanning approx. 10 kb. Primer extension experiments mapped the transcription start point at 298 nt upstream from the predicted start codon. Twenty nt upstream from the polyadenylation site of the gene, an uncanonical polyadenylation signal, AGTAAA, was found. Human PGPx was localized on chromosome 5 band q32 by fluorescence in situ hybridization.
编码人血浆谷胱甘肽过氧化物酶(PGPx)的基因组克隆被分离出来,该酶是血浆中还原脂质氢过氧化物和过氧化氢的主要酶,并测定了5618个核苷酸(nt)。核苷酸序列数据显示,PGPx基因由五个外显子组成,跨度约为10 kb。引物延伸实验将转录起始点定位在预测起始密码子上游298 nt处。在该基因的聚腺苷酸化位点上游20 nt处,发现了一个非典型的聚腺苷酸化信号AGTAAA。通过荧光原位杂交,将人PGPx定位在5号染色体q32带。