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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.
The fresh bee pupa, honey, royal jelly and Apis cerana with wings cut were homogenized, acid treated to pH 5.0 (ACPase, EC 3.1.3.2) was isolated and purified from Apis cerana, and the properties of the enzyme had been studied , then compared the ACPase activities of the four kinds of the homogenate. The Acid phosphatase was partially acquired Apis cerana by homogenate, ammunium sulfate fractionation and gel filtration with Sephadex G 150. purified enzyme moved as a single electrophoretic band in PAGE. The was pH value for the enzymes was pH 4.1. The optomum temperature was about 50 ° C. 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 hig h concentration inhibited it.The ACPase is inactivated by urea.