长牡蛎碱性磷酸酶的分离纯化及部分性质研究  

Purification and characterization of alkaline phospatase form Crassostrea gigas

作　　者：李兴暖[1] 韩雅莉[1] 肖湘[1] 邓瑞鹏[1] 周小朋[1] 管云雁[1] 黄长江[2] 

机构地区：[1]汕头大学理学院生物系,广东汕头515063 [2]汕头大学科技中心海洋生物研究室,广东汕头515063

出　　处：《台湾海峡》2003年第4期482-486,共5页Journal of Oceanography In Taiwan Strait

基　　金：国家自然科学基金资助项目(30271033);广东省重大科技兴海项目(A200005F02)

摘　　要：本文以长牡蛎为酶源提取材料,用正丁醇抽提,硫酸铵分级分离,DEAE-52和Sephadex G-100柱层析,得到一定纯度的碱性磷酸酶,提纯倍数为61.96,比活力达1.326U/mg.该酶的最适pH值9.6,最适温度38℃,初速度6.8μmol/(dm^3·min),米氏常数Km值为1.30mmol/dm^3.实验结果表明,Mg^(2+)对该酶有明显的激活作用;Zn^(2+)、Cu^(2+)、Hg^(2+)对该酶有明显的抑制作用.Crassostrea gigas alkaline phospatase has been isolated and purified by means of the following procedures:n-butanol extraction, ammonium sulfate precipitation,ion exchange chroma-tography on DEAE cellulose column (DEAE-52) ,and gel filtration chrcmatography on Sephadex G-100,the specific activity of the final preparation was up to 1. 326U/mg protein. The optimum pH is 9.6 and the optimum temperature is 38℃.The initial velocity is 6. 8μmol/(dm3·min) and the Michaelis Menten constant (Km) is 1. 30 mmol/dm3. Mg2+ can activate the enzyme, but Zn2+、Cu2+、Hg2+ can obviously inhibit the enzyme activity.

关 键 词：长牡蛎 碱性磷酸酶 分离 纯化 海洋生物化学 

分 类 号：Q556.1[生物学—生物化学] Q959.215.3