The effect of an inhibitor on an enzyme was tested and the experiment gave the results below. If necessary, plot the data (Lineweaver-Burk) and determine, by inspection of the graph, what type of inhibition is involved. [S] (µM) 0.40 0.66 1.00 2.00 V (μmol/min) without Inhibitor 0.45 0.68 0.88 1.25 V (μmol/min) with 25 nM inhibitor 0.32 0.47 0.61 0.85 A. Competitive B. Non-competitive C. Uncompetitive D. There is no inhibitory effect at either 25 nM or 50 nM. Cannot conclude anything from the data or my graph. V (μmol/min) with 50 nM inhibitor 0.18 0.28 0.35 0.50
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- A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).Determine the Ki for the inhibitor at 30 °Cand decide what type of inhibitor is being used. Eo T I S V (g/I) (°C) (mmol/ml) (mmol/ml) (mmol/ml-min) 1.6 30 0.1 2.63 1.6 30 0.033 1.92 1.6 30 0.02 1.47 1.6 30 0.01 0.96 1.6 30 0.005 0.56 1.6 49.6 0.1 5.13 1.6 49.6 0.033 3.70 1.6 49.6 0.01 1.89 1.6 49.6 0.0067 1.43 1.6 49.6 0.005 1.11 0.92 30 0.1 1.64 0.92 30 0.02 0.90 0.92 30 0.01 0.58 0.92 30 0.6 0.1 1.33 0.92 30 0.6 0.033 0.80 0.92 30 0.6 0.02 0.57Calculate the Km of the enzyme with these parameters. kcat = 130s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM
- In an enzyme experiment, when the enzyme is added only to the substrate, the Vmax value is 0.828 and the Km value is 17.76. When the substrate and activator are added to this enzyme, the Vmax is 0.964 and the Km value is 10.6066. When substrate and inhibitor are added to the enzyme, the Vmax value is 0.550 and the Km value is 11.34. Estimate the effect of the substance added. Are these substances suitable activators/inhibitors for the laccase enzyme?An enzymatic reaction follows M-M kinetics with Vmax= 2.5 mol m-3s-1and Km = 5 mM.Calculate the time required for 50% conversion of the substrate in a batch reactor if theinitial substrate concentration is0.2 M.Show your calculation steps.2) Below are kinetic data at three different inhibitor concentrations. Graph the data in an appropriate form to determine whether the inhibitor is competitive or uncompetitive. a (μm) 0.4 0.67 1.00 2.00 v (μM/min) (no inhibitor) 0.22 0.29 0.32 0.40 v (μM/min) (10 nM inhibitor) 0.21 0.26 0.30 0.36 v (μM/min) (20 nM inhibitor) 0.20 0.24 0.28 0.32
- A mixture containing only KCl and NaBr is analyzed by the Mohr Method. A 0.3172-g sample is dissolved in 50 mL water and titrated to the Ag2CrO4 endpoint, requiring 36.85 mL of 0.1120 M AgNO3. A blank titration requires 0.71 mL of titrant to reach the same endpoint. Report the % (w/w) KCl and NaBr in the sample. [Ans . 84.41 % (w /w); 17.59 % (w /w)]The standard curve to determine the amount of betacyanin is shown below. You extracted a red pigment from a beet disc (the mass of a disc is 2 g) using 10 ml of 20% ethanol solution. You measured absorbance of the solution above the beet disc every minute for a total time of 20 minutes. The increase in absorbance was linear during a period of time from 1 min to 10 min. The absorbance at 10 min was 0.8. Calculate the amount of betacyanin extracted from 1g of a beet tissue per minute. Explain your calculations. You can use Excel or a calculator.The concentration of hydrolyzed nitrocefin at each time point for an experiment is given below. Time (min) Concentration (μM) 0.5 6.01 1 11.78 1.5 17.6 2 23.51 2.5 29.58 3 35.31 3.5 39.73 4 44.5 4.5 48.18 5 50.05 5.5 52.72 6 54.01 6.5 55.06 7 55.65 7.5 56.39 8 56.74 8.5 57.49 9 58.03 9.5 58.61 10 58.69 Make a graph that plots the concentration of hydrolyzed nitrocefin (in μM) against time (in seconds) using Excel, R, SPSS or other computable software. Where appropriate, include a trendline that shows the linear range on your graph. Include the equations for the trendlines and the R2 value on the graph. Your graph should also include a title and appropriate titles for the x- and y-axes, with units included where appropriate. To determine the initial velocity of a possible insert in this experiment, you must determine what the linear range is in these data (see note below). Based on your graph, which time points represent a suitable linear…
- Determine the fraction of Vmax that would be obtained when the substrate concentration, [S], is 0.5Km. Vmax fraction: .769Suppose that the data shown in the margin are obtained for an enzyme -catalyzed reaction. [S] (mM) V (mmol/ml min) 0.1 3.33 0.2 5.0 0.5 7.14 0.8 8.00 1.0 8.33 2.0 9.09 a.) Determine the Km and Vmaxb.) Assuming htat the enzyme present in the system had a concentration of 10-6M, calculate the turn -over numberFill up the two missing values inside the two circles knowing that the total reaction volume is 2mL. 1) Dilution fraction 2) Water Don't include units in your answer. Membrane Brillant blueR 1g/L Dilution Sample suspension fraction (μL) (μL) 1) Control ? 0 50 2) 1/200 ? 10 50 3) 1/100 0.01 20 50 4) 1/50 ? 40 50 5) 1/20 100 50 Phosphate pH11, 0.2M (ml) 1 1 1 1 1 Water (mL) 0.95 ? ? ?