Calculated the specific activity (U/mg) of the purified lysozyme fraction having the most activity. Please include Standard curve from an Excel file and handwritten calculation for specific activity. (\epsi = 38,000 M-1 s-1 for lysozyme)
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- 4mL of diluted protein solution was prepared by mixing 200uL of the protein solution with 3.8mL of distilled water. 100uL of this diluted was then mixed with 900uL of Lysozyme solution. Lysozyme activity was measured at 450nm and gave a reading of -0.080 (Abs/min). Calculate the concentration of lysozyme activity in units of abs/min/mL.You are studying the absorbance properties of the COVID-19 virus. You notice at (4.9500x10^-1) absorbance, the molar absorptivity of the G variant is (4.7887x10^5) M1 cm in hexane at (5.3700x10^2) nm. The concentration was determined to be (3.60x10^-4) M. What is the pathlength of the cuvette in nanometers (nm)? Please do not include units in the answer and present your answer in scientific notation. Note: Your answer is assumed to be reduced to the highest power possible. Your Answer: x10 Answer2. Using the following data, determine the Vmax and Km of the enzyme catalyzed reaction: [S] (M) 2.5 X 10-6 4.0 X 106 1 X 105 2 X 10'5 Vo (uM/min) 28 40 70 95 [S] (M) 4 X 105 1 X 10 2 X 10³ 1 X 10² Vo (uM/min) 112 128 139 140
- If %T for sample A is 0.005%T and for sample B it is 25%T at 10 minutes after adding enzyme, which of the two tubes shows enzyme activity? Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a Sample B Sample A Cannot determine without further information7. 116.5 ug of trypsin (MW 23.3 kDa) was mixed in a 1 ml solution with an excess of a peptide substrate. The reaction is stopped after 10 seconds and the amount of cut peptide is measured to be 3.35 umole. The reaction is repeated with [S] - 0.012 M, and the amount of cut peptide is measured to be 1.175 umole in 10 seconds. a) What is the concentration of enzyme present? b) What is Vm ? c) What is KM ? d) What is kcat ?A direct enzyme-linked immunosorbent assay (ELISA) test on a patient's sample is shown below. Development of a strong (dark) color reaction would indicate: 1 Antibody is adsorbed to well. 2 Patient sample is added; complementary antigen binds to antibody. 3 Enzyme-linked antibody specific 4 Enzyme's substrate () is added, for test antigen is added and binds and reaction produces a product that causes a visible color change (O). to antigen, forming sandwich. A low concentration of a specific antigen in the patient's sample O A high concentration of a specific enzyme in the patient's sample The patient's antibody is specific for the enzyme's substrate O A high concentration of a specific antigen in the patient's sample A high concentration of a specific antibody (against the test antigen) in the patient's sample
- You have a treatment process in which a microbial population consumes a substrate (chemical A) according to Monod kinetics, with Hmax=2 d', Ks = 350 mg/L, and Y 0.15 g cells/g A. What biomass concentration (in mg/L) must be maintained to result in a substrate utilization rate of -1000 mg/L- hr for a concentration of A equal to 5000 mg/L? %3D %3!Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minute4. Suppose the data shown below 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 8.0 1.0 8.3 2.0 9.09 a) Plot the data and determine Km and Vmax (please include the plot). b) Assuming the enzyme was used in these reactions at a concentration of 10-6 M, then calculate the turnover number for the enzyme.
- A blood sample is assayed for creatine kinase activity. It is found that after 2 minutes of reaction, 2.98 μmol of creatine phosphate (the product of the reaction) is produced. How many international units of creatine kinase are present in the sample? | IUIf inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM, calculate the new Vmax. Calculate the new Km of the above lactase reaction, with inhibitor X. Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. Inhibitor X exerts which of the following effects on the above enzyme (lactase)?Calculate the value of the denaturation constant kd for a given enzyme, using the equation provided from the text and lecture of kd = Ad e(-Ed/RT) where Ad = 6.1 x 1047 and Ed = 69 kcal/g mole. Then, prepare a plot of per cent enzyme maximal activity vs temperature using an Ea of 23 kcal/gmole, and an enzyme concentration E0 of unity. Note that the y-axis of this plot is a per cent value, so the value of A in the Arrhenius equation does not need to be known in this case. On the denaturation side of the curve, use 5 minutes as the constant exposure time. Use a temperature range of 20 to 50⁰C.