背角无齿蚌碱性碳酸酶的分离、纯化及其动力学研究

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ISOLATION, PURIFICATION AND SOME KINETIC PROPERTIES OF ALKALINE PHOSPHATASE FROM THE MANTLE OF ANODONTA WOODIANA (HEUDE)

摘要: 作者对背角无齿蚌外套膜的碱性磷酸酶(AKP)进行了分离纯化,并对其动力学性质进行了初步研究。外套膜匀浆,经正丁醇抽提、盐析、Sephadex G-100凝胶过滤等步骤,得到了比活力为149.6单位/mg蛋白的酶制品。通过动力学方法测得其最适pH值为9.5,最适温度为40℃,以磷酸苯二钠作底物的Km值为0.57mmol/L.Mg2+、Ca2+对酶有激活作用,而Cu2+、Zn2+、KH2PO4、EDTA和巯基乙醇有抑制作用。

Abstract: The present paper describes the isolation and purification of alkaline phosphatase (AKP) from the mantle of Anodonta woodiata (Heude), and its kinetic property is also examined. The alkaline phosphatase was partially purified from the mantle by homogenation, nbutanol extraction, salting-out and gel filtration with Sephadex G-100. Gained AKP product has a specific activity of 149.6 unit/mg AKP protein. The optimum pH value of the AKP product is 9.5 as hydrolysed in disodium phenyl phosphate and its optimum temperature is 40℃. The Michaelis-Menten constant (Km) is 0.57 mmol/L (on the disodium phenyl phosphate). The AKP was activated by Mg2+ and Ca2+ ions while inhibited by ions of Cu2+, Zn2+ and reagents of KH2PO4, EDTA and ME.