Sjögren S, Ek-Rylander B, Hammarström L
Department of Histology, Dental Faculty, Lund University, Sweden.
Acta Odontol Scand. 1988 Apr;46(2):75-82. doi: 10.3109/00016358809004750.
Alkaline phosphatase (APase) is a plasma membrane-integrated protein with unknown function and is found in many different tissues of the body. It is normally not present in squamous epithelium. Nevertheless, it has been demonstrated in developing rat oral epithelium, where it exists together with several different phosphatases. In this study APase was solubilized from rat buccal mucosa and partially purified by gel chromatography followed by ion-exchange chromatography. Three isoenzymes with similar kinetic characteristics but different sensitivities to heat inactivation were obtained. All three had a pH optimum of 10.2 and a Michaelis-Menten constant of 0.3 mM. Combined chromatographic/electrophoretic and histochemical tissue section analysis of APase isoenzymes indicated that the buccal mucosa of young rats contains three APase isoenzymes, two of which are of epithelial origin and the third of endothelial origin.
碱性磷酸酶（APase）是一种功能未知的整合于质膜的蛋白质，存在于身体的许多不同组织中。它通常不存在于鳞状上皮中。然而，在发育中的大鼠口腔上皮中已证实有碱性磷酸酶，它与几种不同的磷酸酶一起存在。在本研究中，碱性磷酸酶从大鼠颊黏膜中溶解出来，并通过凝胶色谱法随后进行离子交换色谱法进行部分纯化。获得了三种具有相似动力学特征但对热失活敏感性不同的同工酶。所有三种同工酶的最适pH均为10.2，米氏常数为0.3 mM。对碱性磷酸酶同工酶进行的色谱/电泳和组织化学组织切片联合分析表明，幼鼠的颊黏膜含有三种碱性磷酸酶同工酶，其中两种起源于上皮，第三种起源于内皮。
