You make reaction progress curve by plotting absorbance vs time (seconds) and find the equation of the line to be y = -0.00235x + 0.7129. Calculate the U/µL and U/mL of lactate dehydrogenase activity in this fraction. The LDH activity is done identical to what is indicated in the lab manual. Show each step of the calculation from AU/time to M/min, to mol/min, to µmol/min to µmol/min/µL (=U/µL).
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You make reaction progress curve by plotting absorbance vs time (seconds) and find the equation of the line to be y = -0.00235x + 0.7129. Calculate the U/µL and U/mL of lactate dehydrogenase activity in this fraction. The LDH activity is done identical to what is indicated in the lab manual. Show each step of the calculation from AU/time to M/min, to mol/min, to µmol/min to µmol/min/µL (=U/µL).
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- Calculate the Vmax of the above enzyme (lactase). (the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM) 0.125 mM per minute 0.25 mM per minute 0.50 mM per minute 1.25 mM per minute 5.0 mM per minuteYou plot a reaction progress curve and find the equation of the line to be y = -0.0961x + 0.7142. Calculate the U, U/μL and U/mL of lysozyme activity in this fraction. The lysozyme activity is done identical to what is indicated in the lab manual.From your Lineweaver-Burk plot,the vlaues are: Km Vmax Uninhibited 0.09 mmol/L 3.02 min/mmol Inhibited 6.22 mmol/L 9.98 min/mmol By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity.
- Calculate for the water activity of the soy sauce in 80.3% ERH. Suppose the soy sauce is subjected to a storage area with RH of 95.9%. What will be the water activity of the soy sauce?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)Your current Vmax (4x10-3 A/S) from the Michaelis-Menten plot has the units of A/s and was determined using 0.1 mg of ADH in a total volume of 1.25 mL. Use the Beer-Lambert equation followed by simple conversion to express your estimated Vmax in (mol )/s per 1 mg ADH. The molar absorptivity of NADH at 340 nm is 6220 L/(mol*cm).
- Calculate the concentration of p-aminophenol control to match the 0.075 % w/w limit in 200 mg/10 ml Your Answer: 0.0015% show workFigure I shows the Michaelis Menten plot of initial reaction velocity (as percentage of Vmax) versus [S] (concentration) for the carbonic anhydrase reaction in the absence and presence of the inhibitor acetazolamide. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. 100 No inhibitor Acetazolamide 0.2 0.4 0.6 0.8 1 [S] (mM) Figure 1 (i) Compare Vmax and Km of the enzyme without inhibitor and in the presence of acetazolamide. Determine the type of inhibition shown by acetazolamide. Explain your answer. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide in Qla)(i). List down the kinetic properties of these inhibitions. Sketch a graph of I/V versus 1/[S] showing plots in the absence of an inhibitor and in the presence of the types of inhibitors mentioned in Qla)(ii). (iii) V (% of VmaxSuppose 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 number
- You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphataseProline 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?a) Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200 L M-1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) above