Henthorn P S, Raducha M, Edwards Y H, Weiss M J, Slaughter C, Lafferty M A, Harris H
Proc Natl Acad Sci U S A. 1987 Mar;84(5):1234-8. doi: 10.1073/pnas.84.5.1234.
A cDNA clone for human adult intestinal alkaline phosphatase (ALP) [orthophosphoric-monoester phosphohydrolase (alkaline optimum); EC 3.1.3.1] was isolated from a lambda gt11 expression library. The cDNA insert of this clone is 2513 base pairs in length and contains an open reading frame that encodes a 528-amino acid polypeptide. This deduced polypeptide contains the first 40 amino acids of human intestinal ALP, as determined by direct protein sequencing. Intestinal ALP shows 86.5% amino acid identity to placental (type 1) ALP and 56.6% amino acid identity to liver/bone/kidney ALP. In the 3'-untranslated regions, intestinal and placental ALP cDNAs are 73.5% identical (excluding gaps). The evolution of this multigene enzyme family is discussed.
从λgt11表达文库中分离出了人成人肠碱性磷酸酶(ALP)[正磷酸单酯磷酸水解酶(最适pH碱性);EC 3.1.3.1]的cDNA克隆。该克隆的cDNA插入片段长度为2513个碱基对,包含一个编码528个氨基酸多肽的开放阅读框。通过直接蛋白质测序确定,该推导多肽包含人肠ALP的前40个氨基酸。肠ALP与胎盘(1型)ALP的氨基酸同一性为86.5%,与肝/骨/肾ALP的氨基酸同一性为56.6%。在3'-非翻译区,肠和胎盘ALP的cDNA同一性为73.5%(不包括缺口)。本文讨论了这个多基因酶家族的进化。