Here v=d[P]/dt is the rate of formation of product or can be said rate of reaction. If we see the plots at different substrate concentration these are steeply rise initially (around till 50 min) then become almost parallel to the x-axis. it means at some increased time the rate of product formation is decreased. Or the rate is dependent on time or instanteneous concentration of the substrate. So we should take the slope along the time axis with initial periods (the range of 0 min. to 50 min. can be choosed in these particular plots). So we get actual instanteneous rate of the enzymatic reaction during initial period of time. As it is clear from the plots that the slope value will we lowest for 0.5 mM substrate concentration which increases gradually till 10 mM.
Formation of Product by ACE 10 S] (mM) 4 2 0.5 t (min) 50 100 150...
A different experiment yields the following kinetic data Substrate] (mM)Vo (uM/min) no inhibitorVo (uM/min)+7 nM inhibitor 0.02 0.04 0.10 0.25 1.00 2.50 0.8 2.9 8.6 24 36 50 Plot the data for the kinetics of the enzyme (with and without the inhibitor) in a double reciprocal (Lineweaver-Burk) plot. Keep in mind that the x axis is 1/[S] and the y axis is 1/Vo. If you are using Excel you want to choose the (x,y) scatter plot (without a ne). You...
2. hypothesize the best conditions (pH and temperature) under which the enzyme chymotrypsin functions with an appropriate reference. also, hypothesize what will occur in the presence of an inhibitor and the type of inhibition. EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
5) The reaction, 2A + B P (P is the product). proceeds via a rapid pre-equilibrium (with equilibrium constant, K) followed by a slow rate determining step (with rate constant, kz) as shown below: 2A к = Az (fast pre-equilibrium) A2+B Products (slow) Develop an expression for the rate of formation of products as a function of [A], [B], K, and kz 6) The reaction, A+B+C - P(P is the product) proceeds by the following mechanism. k, A+B=0 I+CP "T"...
3. Use the below tables to complete lab calculations on the worksheet on pages 2-6 of this document. You will submit the worksheet via dropbox on Canvas by you assigned lab time the week of March 30th through April 3rd. A document with sample calculations of different concentrations is provided to you on canvas. Enzyme Kinetics Lab Buffer volume (mL) Enzyme Volume (ml) Substrate Volume (ml) TOTAL VOLUME (mL) 0.04 0.5 1.5 0.04 0.25 1.5 0.04 0.1 1.5 0.04 0.05...
Question 1 - Linked Reactions (10 marks) The reaction catalysed by pyruvate kinase is: Phosphoenolpyruvate+ ADPpyruvateATP Keg 3.63 x 105 a) Calculate the AG" for this reaction. Show your working. 3 marks b) The hydrolysis of ATP has following equation: AG 30.5 kJ/mol Calculate the AG" for the following reaction: Phosphoenolpyruvate pyruvateP Show your working. 2 marks c) At 37 °C, the steady-state concentrations of phosphoenolpyruvate, ATP, and ADP have been measured to be 23 HM, 1.85 mM and 140...
Based on the document below, 1. Describe the hypothesis Chaudhuri et al ids attempting to evaluate; in other words, what is the goal of this paper? Why is he writing it? 2. Does the data presented in the paper support the hypothesis stated in the introduction? Explain. 3.According to Chaudhuri, what is the potential role of thew alkaline phosphatase in the cleanup of industrial waste. CHAUDHURI et al: KINETIC BEHAVIOUR OF CALF INTESTINAL ALP WITH PNPP 8.5, 9, 9.5, 10,...