意蜂工蜂酸性磷酸酶的分离纯化及动力学研究  被引量:4

ISOLATION PURIFICTION AND KINETIC PROOERTY STUDY OF ACID PHOSPHATASE FROM APIS CERANA

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作  者:江琰[1] 刘克武[1] 杨守忠[1] 张洪渊[1] 魏炜[1] 赵欣平[1] 刘晓雯[1] 闵丽娥[1] 张斌[1] 喻东[1] 

机构地区:[1]四川大学生命科学学院,成都610064

出  处:《四川大学学报(自然科学版)》2001年第5期776-780,共5页Journal of Sichuan University(Natural Science Edition)

摘  要:Acid phosphatase (ACPase, E.C.3.1.3.2) was isolated and purified from Apis cerana, and properties of the enzyme had been studied. The fresh bee pupa,honey,royal jelly and Apis cerana with wings cut were homogenized, acid treated to pH 5.0, then compared the ACPase activities of the four kinds of the homogenate. The Acid phosphatase was partially obtained Apis cerana by homogenate, ammunium sulfate fractionation and gel filtration with Sephadex G 150.The purified enzyme moved as a single electrophoretic band in PAGE. The purification multiple was 16.54,and the specific activity was 3.47U/mg.Pr with pNPP as its substrate. The optimum pH value for the enzymes was pH 4.1. The optomum temperature was about 50℃. The Michaelis Menten constant ( K m ) was 2.32×10 -4 mol/L on the pNPP. The ACPase was activated by Zn 2+ ,Mg 2+ and K +,while inhibited by ions of Cu 2+ ,Fe 3+ and Cr 3+ . Pb 2+ in low concentration activated the enzyme and in high concentration inhibited it.The ACPase is inactivated by urea.Acid phosphatase (ACPase, E.C.3.1.3.2) was isolated and purified from Apis cerana, and properties of the enzyme had been studied. The fresh bee pupa,honey,royal jelly and Apis cerana with wings cut were homogenized, acid treated to pH 5.0, then compared the ACPase activities of the four kinds of the homogenate. The Acid phosphatase was partially obtained Apis cerana by homogenate, ammunium sulfate fractionation and gel filtration with Sephadex G 150.The purified enzyme moved as a single electrophoretic band in PAGE. The purification multiple was 16.54,and the specific activity was 3.47U/mg.Pr with pNPP as its substrate. The optimum pH value for the enzymes was pH 4.1. The optomum temperature was about 50℃. The Michaelis Menten constant ( K m ) was 2.32×10 -4 mol/L on the pNPP. The ACPase was activated by Zn 2+ ,Mg 2+ and K +,while inhibited by ions of Cu 2+ ,Fe 3+ and Cr 3+ . Pb 2+ in low concentration activated the enzyme and in high concentration inhibited it.The ACPase is inactivated by urea.

关 键 词:意蜂工蜂 酸性磷酸酶 分离纯化 动力学 蜜蜂 

分 类 号:S893.3[农业科学—特种经济动物饲养]

 

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