碱性磷酸酶、钙ATP酶与植酸酶之间的关系。

The relationship of alkaline phosphatase, CaATPase, and phytase.

作者信息

Williams S A, Culp J S, Butler L G

出版信息

Arch Biochem Biophys. 1985 Aug 15;241(1):10-3. doi: 10.1016/0003-9861(85)90354-6.

Abstract

Alkaline phosphatase, highly purified from bovine intestinal mucosa, has significant hydrolytic activity against phytate and CaATP. Phytase and CaATPase activities require quite different assay conditions than those which are optimal for conventional alkaline phosphatase substrates such as 4-nitrophenyl phosphate. We have used affinity chromatography and antibody recognition to demonstrate that the phytase and CaATPase activities are not due to contaminating enzymes, but are intrinsic activities of intestinal alkaline phosphatase. All of the phytase and CaATPase activities present in crude extracts of bovine intestinal mucosa can be accounted for by alkaline phosphatase. Apparently neither phytase nor CaATPase exist in this tissue as independent enzymes. Specific substrates which require assay conditions quite different from the conventional 4-nitrophenyl phosphate substrate may account for the physiological function of "alkaline phosphatase."

摘要

从牛小肠黏膜中高度纯化得到的碱性磷酸酶，对植酸和CaATP具有显著的水解活性。与针对传统碱性磷酸酶底物（如对硝基苯磷酸酯）的最佳检测条件相比，植酸酶和CaATP酶活性所需的检测条件大不相同。我们利用亲和层析和抗体识别来证明，植酸酶和CaATP酶活性并非由污染酶导致，而是肠碱性磷酸酶的固有活性。牛小肠黏膜粗提物中存在的所有植酸酶和CaATP酶活性都可由碱性磷酸酶来解释。显然，在该组织中，植酸酶和CaATP酶都不是独立存在的酶。需要与传统对硝基苯磷酸酯底物截然不同的检测条件的特异性底物，可能解释了“碱性磷酸酶”的生理功能。