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细胞生物化学实验教材Exp 3-Determination of Km -Lei Zhang-updated.ppt
Determination of Km of Alkaline Phosphatase (AKP) ;Overview;Objective;Principles;Michaelis-Menten Equation;At low concentrations of the substrate [S], velocity (V) is proportional to [S], is a usual features of a first order reaction.
With the increase of substrate concentration, V does not increase proportionally to [S]. At substrate concentrations far higher than Km, ([S]Km), the curve approaches to a plateau. The reaction becomes nearly independent of the substrate concentration and shows zero-order kinetics.
When the enzyme is saturated by substrate, almost all enzyme molecules are present as enzyme-substrate complex and the reaction is no longer limited by substrate availability but by the amount and the turnover number of the enzyme.;Lineweaver-Burk Double-reciprocal Plot;When used for determining the type of enzyme inhibition, the Lineweaver–Burk plot can distinguish competitive and non-competitive inhibitors of enzyme.;Alkaline Phosphatase (AKP);In this experiment, a substrate called disodium phenylphosphate is used to measure the activity of AKP. Disodium phenylphosphate can be hydrolyzed by AKP and produce phenol and phosphates.
The higher activity of AKP the more phenol is produced. So the concentration of phenol varies in proportion with the activity of AKP.
Phenol and 4-aminoantipyrine can be oxidized to quinone derivatives. The more phenol active as substrate, the more quinone derivatives are produced, which are red compounds with maximum absorption peak at 510nm.;Procedure;(2) mix test tubes 1-6 well and incubate at 37℃ for 15 minutes.
(3) add 1.1ml of alkaline solution into each tube to terminate reaction.
(4) add 1.0ml of 0.3% 4-aminoantipyrine and 2.0ml of 0.5% potassium ferricyanide into each tubes, mix well then place them at RT for 10 minutes.
(5) #6 and 6’ tubes are as blank. Measure the A510 of each samples using the spectrophotometer and the blank tube is used for the zero setting.
(6) Plot 1/A510 against 1/[S] and calculate Km.;Plot a
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