The Infection Of Effectors On The Activity Of Alkaline Phosphatase From Haliotis Diversicolor

Haliotis diversicolor is the main breed in the south of China. It has high value in economic and medicinal properties. Alkaline phosphatase (ALPase, EC.3.1.3.1) is a metabolism enzyme which catalyzes the nonspecific hydrolysis of phosphate monoesters.It is closely related to the growth of Haliotis diversicolor. In this research we study The infection of the effectors including phosphate and it's analogues ,formamide ,dimethyl formamide , dioxane, dimethyl sulfoxide, mercapto-compounds, sodium dodecyl sulfate (SDS) and Potassium bisperoxo (oxalato)oxotitanate[PV (ox) ], sodium bisperoxo(2,2'-bipyridine) oxotitanate [PV(bipy)] and Potassium bisperoxo(l,10-phenanthroline ) oxotitanate [PV(phen)] on the activity of alkaline phosphatase from Haliotis diversicolor.Study on the basal character and dynamics character of enzymology,the impacts from kinds of contamination on it and the impact on the growth or disease of Haliotis diversicolor from ALPase is to offer important consulting and instructing informations for Haliotis diversicolor aquiculture.The results showed that:1.The inactivation effects of alkaline phosphatase (ALPase) from Haliotis diversicolor in organic solvents (dimethyl formamide, dioxane, dimethyl sulfoxide), phosphate and it's analogues , mercapto-compounds (DTT and ME ), and PV solvents have been studied using the kinetic method of Lineweaver-Burk plot. And their inhibition types and inhibition constants have been determined. The results showed that the inactivation of the enzyme in these effectors was reversible reaction. The inactivation of the enzyme in phosphate and it's analogues , PV(bipy) and PV(phen) solvents belonged to be competitive type.The inactivation of the enzyme in mercapto-compounds and dioxane belonged to be noncompetitive type, while that in dimethyl formamide, dimethyl sulfoxide and PV(ox) solvents was mixed type.2. The inactivations of the enzyme by DTT and ME have been studied using the kinetic method of the substrate reaction during inhibition of enzyme activity previously described by Tsou. The microscopic rate constants for the reaction of these inactivators with free enzyme and the enzyme-substrate complex were determined. Comparison of...