Title :
Isolation Purification and Some Properties of Alkaline Phosphatase from Hypophthalmichthys Molitrix Cuv.et Val
Author :
Tang Yun-Ming ; Xu Min ; Yao, Ma ; Du Hong-xuan ; Cheng Rong-chan ; Yang Qin
Author_Institution :
Sch. of Life Sci., Southwest China Univ., Chongqing
Abstract :
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 separated through DEAE-Sepharose and Sephacryl S-200. The purification folds was 150.08,while the specific activity was 4031.15 U/mg.The properties research suggested that the optimal pH and temperature were pH10.2 and 40degC respectively,and the AKP was unstable when the pH was out of range of pH7 to pH12, or the temperature was higher than 50degC.The data showed the Km value of the AKP was 4.73 mmol/L. Also,some ions had effect on the activity of AKP,such as Mg2+ which activated the AKP and Zn2+ which inhibited the AKP.
Keywords :
biochemistry; chemical technology; organic compounds; pharmaceuticals; purification; DEAE-sepharose; Hypophthalmichthys molitrix; Tris-HCl buffer; alkaline phosphatase; isolation; n-butanol; pH 7 to 12; purification; sephacryl S-200; Animals; Biochemistry; Filtration; Ice; Kinetic theory; Proteins; Purification; Solvents; Stability; Temperature distribution;
Conference_Titel :
Bioinformatics and Biomedical Engineering, 2008. ICBBE 2008. The 2nd International Conference on
Conference_Location :
Shanghai
Print_ISBN :
978-1-4244-1747-6
Electronic_ISBN :
978-1-4244-1748-3
DOI :
10.1109/ICBBE.2008.73
