3. Show that the inverse of equation 29-78 in the textbook gives the Lineweaver-Burk Equation. The hydration of CO2 is catalyzed by the enzyme carbonic anhydrase. For a total enzyme concentration of 2.32 x 10-⁹ M, the following data were obtained. [CO2]o (M) 0.00125 0.00250 0.00500 0.02000 v (M/s) 2.78 x 10-5 5.00 x 10-5 8.33 x 10-5 1.66 x 10-4 Plot these according to the Burke-Lineweaver Equation and determine the values of Km, the Michaelis constant, and k2, the rate constant for product formation from the enzyme-substrate complex from the slope and intercept of the plotted data.
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- Proline racemase catalyzes the conversion between L-proline and D-proline. The Km and kcat for this reaction are 0.15 M and 550/sec respectively. If the enzyme concentration is 1.45 X 10-5 mmole/ml what is the Vmax of this reaction?The equation of the double reciprocal plot is y = 0.5294 x + 1.4960. What is the value of vmax (in M/s)? The substrate concentration is given in units of molarity (M) and reaction velocity has units of molarity per second (M/s). (Report to three significant figures)The effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shown below in Table 1. The temperature coefficient, Q10 is the factor by which the rate increases by raising the temperature 10°C. The universal gas constant, R is 8.314 J/mol.K. (a) (b) Table 1: Data of Vmax over temperature T (°C) 20 30 35 40 45 Vmax (umoles/min.mg protein) 4.50 8.65 11.80 15.96 21.36 Plot the graph of In Vm vs 1/T using any spreadsheet software (include all appropriate labels and equation). Calculate the activation energy Ea and temperature coefficient Q10.
- The following data were obtained for a reaction that catalyzed by an enzyme: Initial concentration of 0.141 0.109 0.077 0.040 0.028 0.020 0.016 the enzyme [S], mol L- Relative velocity, V 22.0 20.5 19.0 12.5 9.0 7.0 6.0 For this reaction, the rate is found experimentally to follow the Michaelis-Menten equation: Vmax[S] Vo = Км+[S] (1) Transform the above equation into a straight-line equation. By plotting a suitable graph, determine the Michaelis constant (KM) and the maximal velocity (Vmax) for the above reaction. Determine the Vmax value when [S] = KM.5) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for the rates of reaction with glucopyranoside for various substrate concentrations was obtained. By constructing a Leaver-Burk plot, determine the value of the Michaelis constant. [S]/ (10-6 mol dm-3) v/ (10-3 mol dm-3 s-1) 1.00 2.00 3.00 4.00 16.7 33.3 41.1 49.8Tirofiban (C22H36N₂O5S MWt = 440.6) is present as tirofiban HCI monohydrate MWt=495.1) at 0.281 mg/mL in a concentrated solution. (C22H36N2O5S.HCI.H₂O A solution for infusion is prepared by extracting 50 mL from a 250 mL bag of 5% glucose s and adding 50 mL of concentrated solution. Sonya who weighs weighs 60 kg requires a tirofiban dose of 0.4 mcg/kg/min for 30 minute- What volume would remain after 30 minutes? Answer: 94.53 mL X The correct answer is: 236 mL
- In your acid phosphatase enzyme kinetics lab, you constructed a Lineweaver-Burk plot. Lefs assume that you graphicaly obtain 1/Vmax - 9.33 (umoliey and -1Km--0.012 M. Which of the following is correct? A) Vmax = 9.33 (no units) B) Km = 0.012 (no units) C) Vmax = (1/Vru" = 0.107 umolis D) Km =-14-1K = 83.3 pM E) Both C) and D) are correctFor the following results of Thermodynamics of Borax Solubility, the volume of Borax solution titrated by HCI is 8.00 mL. Table 1. Volumes of hydrochloric acid required to titrate a saturated borax solution at varying temperatures. The hydrochloric acid was a solution standardized at 0.2912 M. Borax Volume added (mL) Temp. (°C) 8.00 8.00 8.00 8.00 8.00 HCI Volume (mL) 50.5 33.75 40.7 27.02 30.0 17.95 20.2 13.43 10.3 8.55 Using Thermodynamic formula (R= 8.31 J/K•mol) and the above results, (e) AS° = (J/K⚫mol) Type your answer...For the following results of Thermodynamics of Borax Solubility, the volume of Borax solution titrated by HCI is 8.00 mL. Table 1. Volumes of hydrochloric acid required to titrate a saturated borax solution at varying temperatures. The hydrochloric acid was a solution standardized at 0.2912 M. Borax Volume added (mL) Temp. (°C) 8.00 8.00 8.00 8.00 8.00 HCI Volume (mL) 50.5 33.75 40.7 27.02 30.0 17.95 20.2 13.43 10.3 8.55 Using Thermodynamic formula (R= 8.31 J/K⚫mol) and the above results, (b) What is the y-intercept of the best fitting line for this data? Type your answer...
- The standard state free energy of hydrolysis of acetyl phosphate isΔG° = -42.3 kJ/mol. Acetyl-P + H2O acetate + Pi Calculate the free energy change for the acetyl phosphate hydrolysis in a solution of 2 mM acetate, 2 mM phosphate and 3 nM acetyl phosphate.In vitro experiments are conducted at pH = 7.4 to simulate physiological conditions. A phosphate buffer system is often used. H₂PO → H₂PO¹²¯ +H+ pK₁ = 7.2 a. What must be the ratio of the concentrations of HPO to H₂POд ions? b. What mass of NaH2PO4 must be added to 500.0 mL of 0.10 M Na₂HPO4 (aq) in the preparation of the buffered solution?[References) The AG" for the reaction ATP + H₂O ADP + P + H+ is -30.5 kJ mol'¹, Other organophosphate species also undergo hydrolysis of the phosphate moiety via a similar reaction. Determine the value of AG for the following reactions and indicate if the reaction will proceed spontaneously in the direction written if the reactants and products are initially in a 1:1 molar ratio. a. ATP + Glucose ADP+ Glucose-1-phosphate AG⁹¹ = kJ mol-1 The reaction is (The hydrolysis reaction for glucose-1-phosphate is Glucose-1-phosphate + H₂0 Glucose + P + H+; AG-20.9 kJ mol ¹.) b. ATP + Glutamate Carbamoyl phosphate + ADP AG The reaction is kJ mol-1 (The hydrolysis reaction for carbamoyl phosphate is Carbamoyl phosphate + H₂0 Glutamate + P, + H+ ; AG¹ = -51.4 kJ mol ¹.) Submit Answer Try Another Version 3 item attempts remaining