ISOLATION, PURIFICATION AND SOME PROPERTIES OF ALKALINE PHOSPHATASE FROM Hypophthalmichthys molitriz Cuv. et Val
Abstracted by Tris-HCl buffer,pH8.5, treated by n-butanol, and fractioned by (NH4)2SO4 60%, the alkaline phosphatase(AKP) from guts of Hypophthalmichthys molitrix Cuv.et Val was seperated through DEAE-Sepharose and Sephacryl S-200.The purification folds was 150.08,while the specific activity was 4031.15 U/mg.The properties reasearch suggested that the optimal pH and temperature were pH10.2 and 40 respectively, and the AKP was unstable when the pH was out of range of pH7 to pH12, or the temperature was higher than 50.The data showed the Km value of the AKP was 4.73mmol/L.Also,some ions had effect on the activity of AKP,such as Mg2+which actvited the AKP and Zn2+ which inhibited the AKP.
Alkaline phosphatase Isolation Purification Properties Hypophthalmichthys molitriz Cuv.et Val
TANG Yun-Ming Xu Min Ma Yao Du Hong-xuan Cheng Rong-chan Yang Qin
School of Life Science, Southwest China University, Chongqing, china 400715
国际会议
上海
英文
282-285
2008-05-16(万方平台首次上网日期,不代表论文的发表时间)