人肠碱性磷酸酶cDNA的克隆与测序
Cloning and sequencing of human intestinal alkaline phosphatase cDNA.
作者信息
Berger J, Garattini E, Hua J C, Udenfriend S
出版信息
Proc Natl Acad Sci U S A. 1987 Feb;84(3):695-8. doi: 10.1073/pnas.84.3.695.
Abstract
Partial protein sequence data obtained on intestinal alkaline phosphatase indicated a high degree of homology with the reported sequence of the placental isoenzyme. Accordingly, placental alkaline phosphatase cDNA was cloned and used as a probe to clone intestinal alkaline phosphatase cDNA. The latter is somewhat larger (3.1 kilobases) than the cDNA for the placental isozyme (2.8 kilobases). Although the 3' untranslated regions are quite different, there is almost 90% homology in the translated regions of the two isozymes. There are, however, significant differences at their amino and carboxyl termini and a substitution of an alanine in intestinal alkaline phosphatase for a glycine in the active site of the placental isozyme.
摘要
通过对肠碱性磷酸酶获得的部分蛋白质序列数据表明，其与已报道的胎盘同工酶序列具有高度同源性。因此，克隆了胎盘碱性磷酸酶cDNA，并将其用作探针来克隆肠碱性磷酸酶cDNA。后者（3.1千碱基）比胎盘同工酶的cDNA（2.8千碱基）稍大。虽然3'非翻译区有很大差异，但两种同工酶的翻译区几乎有90%的同源性。然而，它们的氨基和羧基末端存在显著差异，并且肠碱性磷酸酶中的一个丙氨酸替代了胎盘同工酶活性位点中的一个甘氨酸。
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