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 (uM/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
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- 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 0.571. The antibacterial activity of flavonoids was tested against the bacterial strain, Escherichia coli. The minimum inhibitory concentration at which 50% of the compounds were inhibited (MIC50) are presented in the table below for some of the compounds. Table 1: Antibacterial activity of flavonoids tested against E. coli Compound MIC50 (µg/mL) Kaempferol 25.50 Quercetin 35.76 36.72 67.25 137.10 156.34 238.94 320.88 Compound X Luteolin Tangeritin 5,6,7,4'-Tetramethoxyflavone Genistin Genistein 1.4 If galangin were tested, how would its antibacterial activity compare to that of the other flavonoids? Explain your answer.Accelerated Stability Testing Data Determine the expiration date of a drug product with the initial drug concentration of 50 mg/tablet using the following accelerated stability testing data: log Temp Rate Constant (1/min) 1/T (oC) 70 1.73E-05 80 3.38E-05 90 6.45E-05 Reaction Kinetics - Accelerated Stability Testing log In k Rate Constant Temp (oC) Temp (к) (1/min) (1/K) k 70 1.73E-05 80 3.38E-05 90 6.45E-05
- 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).1. Inhibitor Impact Factor Practice calculations with the inhibitor impact factor (IIF).(a) For Ki = 2 μM and [I] = 0.1 μM, what is IIF?(b) For Ki = 2 μM and [I] = 10 μM, what is IIF?(c) Calculate impact on KM-app and Vmax-app for a competitive inhibitor for the conditiondescribed in (a) and as described in part (b).(d) Calculate impact on KM-app and Vmax-app for a non-competitive inhibitor for the conditiondescribed in (a) and as described in part (b).(e) Briefly explain in terms of molecules why the condition described in (a) has a negligibleimpact on enzyme performance AND why the condition described in (b) has a much largerimpact on enzyme performance. Pictures and words.Paclitaxel is used to treat ovarian cancer by infusion at a concentration of 0.6 mg/mL over 24 hours. A dose of 135 mg/m² has been prescribed for Sero. Sero is 1.06 m tall and weighs 92 kg. Paclitaxel comes in vials of 150 mg/25 mL. Calculate the volume of 5%w/v glucose solution that would be required to dilute the concentrated solution to prepare an paclitaxel solution of the required strength.
- Paclitaxel is used to treat ovarian cancer by infusion at a concentration of 0.6 mg/mL over 24 hours. A dose of 135 mg/m² has been prescribed for Sero. Sero is 1.06 m tall and weighs 92 kg. Paclitaxel comes in vials of 150 mg/25 mL. Calculate the volume of 5%w/v glucose solution that would be required to dilute the concentrated solution to prepare an paclitaxel solution of the required strength. Answer: You did not give the correct unit. The correct answer is: 333 mL XYou are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μMAerobic degradation of an organic compound by mixed cultureof organism in wastewater can be represented by following reaction. C3H6O3 + a O2 + b NH3 → c C5H7NO2 + d H2o + e CO2 A. Determine a, b, c, d and e, if YX/S = 0.4 d X/g S. B. Determine the yield coefficients YX/O2 and YX/NH3. C. Determine the degree of reductions for the substrate, bacteria and RQ for the organisms
- in food microbiology, how do you compute for concentration (M) and absorbance (A) of peroxidase activity on hydrogen peroxide at different pH values? (wavelength used = 415nm). can you please explain the calculations thank you if given: Temperature = 75 C Molar absorptivity coefficient = 10.5 Path length (cm) = 2 I = transmitted light = 0.45Phenylephrine and nafazolin solutions are used as decongestants to relieve nasal congestion. Your patient has been given the following prescription below. You need to prepare 100 g of this nasal spray and make it isotonic. 1. There is an available 25% w/w Phenylephrine solution in the pharmacy. How many g of this solution will you need to supply the needed 0.5% of the patient? A. 1.0 g В. 1.5 g С. 2.0 g D. 4.0 g 2. Given the amount calculated on the previous item, and if the E value of phenylephrine HCl is 0.32, calculate its corresponding sodium chloride tonicic equivalent. А. 0.16 B. 0.64 С. 1.60 D. 6.40 3. If the E value of nafazolin is 0.27, what is the sodium chloride tonicic equivalent of the patient's needed nafazolin? A. 0.0135 B. 0.1350 1.3500 D. 13.500 4. What is the combined sodium chloride tonicic equivalent of the remaining ingredients (edetate disodium (E =0.24) and sodium metabisulfite (E = 0.7)? A. 1.060 B. 0.106 С. 1.290 D. 0.129 5. To make the solution isotonic, what…CHEM151/251 Biochemistry 1 a. Determine Km 1. The following data were obtained for a competitive inhibition study in which the [I] = 3 µM for each determination of vo in the presence of inhibitor. The Vmax = 200 μM P/min for both data sets. 200 Vo (UM P/min) 8 8 8 8 8 8 8 8 8 180 160 140 120 100 40 Name (Print)/ID #: the absence of inhibitor. Participation Question # 10 No Inhibitor 50 +Inhibitor 100 [Substrate] (UM) 150 b. Determine Km, app for the data obtained in presence of inhibitor. 200 c. Calculate the value for Ki. Note: a = 1 + [I]/Ki and a¹ = 1 + [I]/Ki*. for the data obtained in