Mulivor R A, Hannig V L, Harris H
Proc Natl Acad Sci U S A. 1978 Aug;75(8):3909-12. doi: 10.1073/pnas.75.8.3909.
Starch gel electrophoresis and inhibition studies with L-phenylalanine, L-homoarginine, L-leucine, L-leucylglycylglycine, and L-phenylalanylglycylglycine were carried out on a series of human alkaline phosphatases [orthophosphoric-monoester phosphohydrolase (alkaline optimum); EC 3.1.3.1] derived from fetal and adult liver, kidney, bone, and intestine. No differences between adult and fetal liver, kidney, or bone alkaline phosphatases were observed by either electrophoretic or inhibition studies. However, the fetal intestinal enzyme could be clearly distinguished from the adult intestinal enzyme by its greater anodal electrophoretic mobility and its retardation after treatment with neuraminidase. Even after extensive neuraminidase treatment, its anodal mobility was still slightly greater than that of adult intestinal alkaline phosphatase. Fetal and adult intestinal enzymes showed the same inhibition profiles with the series of inhibitors both before and after treatment with neuraminidase. A survey of intestinal samples from fetuses and premature infants of various gestational ages indicated that the changeover from the synthesis of fetal to adult intestinal enzyme begins at about 28-32 weeks of gestation. The difference between the fetal and adult forms of intestinal alkaline phosphatase may represent the expression of different gene loci or a difference in post-translational modification.
对一系列源自胎儿和成人肝脏、肾脏、骨骼及肠道的人碱性磷酸酶[正磷酸单酯磷酸水解酶（最适碱性）；EC 3.1.3.1]进行了淀粉凝胶电泳，并使用L-苯丙氨酸、L-高精氨酸、L-亮氨酸、L-亮氨酰甘氨酰甘氨酸和L-苯丙氨酰甘氨酰甘氨酸进行了抑制研究。无论是电泳研究还是抑制研究，均未观察到成人与胎儿肝脏、肾脏或骨骼碱性磷酸酶之间存在差异。然而，胎儿肠道酶通过其更大的阳极电泳迁移率以及用神经氨酸酶处理后的迁移延迟，可与成人肠道酶明显区分开来。即使经过广泛的神经氨酸酶处理，其阳极迁移率仍略高于成人肠道碱性磷酸酶。胎儿和成人肠道酶在用神经氨酸酶处理前后，对一系列抑制剂均显示出相同的抑制谱。对不同孕周的胎儿和早产儿的肠道样本进行的一项调查表明，从胎儿肠道酶合成向成人肠道酶合成的转变大约在妊娠28 - 32周开始。胎儿和成人形式的肠道碱性磷酸酶之间的差异可能代表不同基因位点的表达或翻译后修饰的差异。
