BMI_Lab5EnzymeKinetics

BMI_Lab5EnzymeKinetics - Laboratory V Topic: Principle: All...

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Laboratory V Topic : Enzyme Kinetics Principle : All enzymes show distinct kinetic features. If we plot a graph of the velocity of the enzyme reaction (V 0 ) vs the enzyme substrate [S] using a constant enzyme concentration , it appears as a hyperbola. This plot is mathematically described by Michealis Menten equation and useful to compare the activity of enzymes. During the initial period of an enzyme reaction, there is an excess of enzyme as compared to the substrate. Hence, the reaction velocity increases dependent on the substrate concentration. This is described as the initial velocity . As the reaction proceeds, all the enzyme sites get occupied until the velocity reaches a maximum velocity ( Vmax ). The reaction then continues at a steady state at the maximum velocity. The Km is determined by drawing a Michealis Menten graph or using the Michealis Menten equation. The concentration of the substrate that will produce half the Vmax is known as Km . An enzyme with smaller Kms are more active than enzymes with higher Km values. As the substrate is used up, its concentration decreases, and the velocity of the reaction begins to slow down. In today’s exercise, we will look at the kinetics of Acid phosphatase enzyme. Enzyme acid phosphatase catalysis the hydrolysis of p-nitrophenyl phosphate disodium (PNPP Na 2 ). The enzymatic reaction produces p-nitrophenol (PNP) and phosphate. The enzyme works optimally in an acidic pH (pH 4.8) and at 37 ° C. The lab exercise has four parts. a)
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BMI_Lab5EnzymeKinetics - Laboratory V Topic: Principle: All...

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