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- answer the following questioms.. 1.What is the action of invertase?2.What is the reagent used to detect glucose in the detection of invertase? What is its principle?Determine a molecular cause that allows explaining the BIOCHEMICAL alterations found in the following patient; Determine their estimated 10-year cardiovascular risk. A 37-year-old patient, a woman who has smoked for 10 years, consulted for malaise, headache, nausea, and fatigue. The medical examination found tendon xanthomas, skin xanthomas, signs of atherosclerosis. Laboratory test Glycemia 90 mg/dL, total cholesterol 560 mg//dL, TAG 230 mg/dL, cHDL 33 mg/dl.5. The data in the table below were collected during a laboratory session assaying for thekinetics of Acid Phosphatase. Using a simple flow diagram, show how you would design theexperiment and focus on the principles of the assay and the major components for theexperimental design. Concentration (mM) Absorbance1 (410nm) Absorbance2 (410nm)0 0.007 0.0081 0.051 0.0672 0.078 0.0965 0.168 0.1558 0.234 0.25210 0.297 0.31620 0.523 0.514 30 0.759 0.719
- after a 5 g onion sample is divided into two equal parts, heat treatment to one of these partsit is being implemented. Then both heat-treated and non-treated parts are 10 times their weightit is ground in an environment containing as much buffer and the determination of pyruvate in the supernatants obtainedit's being done.a) As a result of measurements taken at 520 nm; absorbance value for the heat-treated sample;it was found that the absorbance value in the sample that was not heat treated was 0.123 and the absorbance value in the sample that was not heat treated was 0.520.The equation of the calibration accuracy for pyruvate is that y = 0.1367x – 0.001 (nmol/mL)according to the onion sample; a) independent of alinase activity; b) dependent on alinase activityand c) calculate the total pyruvate amounts in terms of nmol/g of onion.b) How is there a relationship between the activity of the enzyme allinase in onions and the amount of pyruvate?Dec,please explain.Explain how the Kirby-Bauer test works and what information it provides. Define minimum inhibitory concentration (MIC). Describe how the E-test works and what information it provides.Example of a Protein Purification Scheme: Purification of the Enzyme Xanthine Dehydrogenase from a Fungus Volume Total Total Specific Percent Fraction (mL) Protein (mg) Activity Activity Recovery 1. Crude extract 2. Salt precipitate 3. Ion-exchange chromatography |4. Molecular-sieve chromatography 5. Immunoaffinity chromatography 3,800 22,800 2,460 0.108 100 165 2,800 1,190 0.425 48 65 100 720 7.2 29 40 14.5 23 1.8 275 152.108 11 Calculate the specific activity of step#4. Note that percent recovery=% Yield.
- 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 XPaclitaxel 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.Data from enzyme inhibition are used to determine a Kmapp and Vmax PP. Comparison of these values with assays run without inhibitor are used to understand how the inhibition is occurring. This is useful for better understanding the active site as well as the practical aspect of pharmaceutical drugs. Below are idealized Line-Weaver Burke plots of different types of inhibitors. Comnetitive Uncomnetitive Mixed +Inh +Inh 4Inh Anh Inh Anh [S] [S] [S] a. How does the value of Vmax for the enzyme compare to the Vmax PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed b. How does the value of Km for the enzyme compare to the Km PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed c. For each situation in Model 1, consider an inhibitor that is better than the one shown on the graph. Answer the following questions for each type of inhibition: i. How would the KmPP change? ii. How would the Vmax PP change?