1) Tyrosinase enzyme activity is assayed by monitoring the oxidation of 3, 4-dihydroxyphenylalanine (dopa) to the red-colored dopachrome. a) Calculate the tyrosinase activity (U/mL) by using the experimental data given below: &=3600 M¹ cm ¹ (molar absorption coefficient for the product dopachrome) v=0.004 L (final volume in the cuvette) time (min) 0 0.5 1 1.5 2 2.5 3 A at 475 nm 0.1091 10.219 0.3186 0.4106 0.4956 0.5724 0.6451 b) If the tyrosinase concentration in the medium is 0.2 mg/mL, find the specific enzyme activity.
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- The plasma profiles of codeine (COD) and metabolites for 2 individuals (labeled A and B) are shown below. The X-axis is time in hours after an oral dose of codeine. [M=morphine; C6G=COD-6-glucuronide; M3G = morphine-3-glucuronide; NM (ignore)]. Note the data is shown on a log scale on the Y-axis. (A) Which individual is the poor metabolizer? Explain how you know this from the profiles? (B) Is this a problem for cough suppression? Explain. -CH HO Codeine COD 10 000 1000 C6G COD 100 M3G M6G NM 10 M 10 20 30 0 10 20 30 Plasma concentration (nmol I-)Tyrosinase enzyme activity is assayed by monitoring the oxidation of 3, 4-dihydroxyphenylalanine (dopa) to the red-colored dopachrome. Calculate the tyrosinase activity (U/mL) by using the experimental data given belowAn experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate) with serum enzymes (Eadie, 1949). In the experiment, two experiments were conducted, namely experiment 1 without using a prostigmine inhibitor and experiment 2 using a prostigmine inhibitor at 1.5 x 10^-7 mol/l. the data obtained are: a. Is prostigmine competitive or noncompetitive inhibitor? b. determine the value of km and rmax for the two experiments, compare
- 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.Hemoglobin is the oxygen carrier in the blood. What is the effect of each of the following treatments on the oxygen affinity of hemoglobin in vitro and how do these changes impact the T state vs. R state of the enzyme? A) Decrease in pH from 7.4 to 7.2. B) Increase in 2,3-BPG concentration.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 enzyme serine hydroxymethy ltransferase (SHMT) catalyses the conversion of serine into glycine. The fo llowing table gives the initial rates, vo, for the SHMT-catalysed reaction of the substrate serine at var ious concentratio ns of serine, lSI.[S]/(mmol dm-3) 10 20 30 40vo(μmol dm-3 s-1) 1.63 2.94 4.10 4.95Use the data to determine the values of the MichaelisMenten constant, the maximum velocity of the reaction, and the maximum turnover number of the enzyme.1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of cabobenzoxyglycyl-L-tryptophan) Plot these results using a lineweaver-Burk method, and determine values for Km and Vmax. substrate concenrate(mM) Velocity(mM.sec-1) 2,5 0.024 5 0.036 10 0.053 15 0.060 20 0.061 25 0.062You 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).
- 1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of cabobenzoxyglycyl-L-tryptophan) Plot these results using a lineweaver-Burk method, and determine values for Km and Vmax. substrate concenrate(mM) Velocity(mM.sec-1) 2,5 0.024 5 0.036 10 0.053 15 0.060 20 0.061 25 0.062 1.2) If the Km of an enzyme for it's substrate remains constant as the concentration of the inhibitor icreaces, what can be said about the mode of inhibition and why? 1.3) calculate the turnover number for an enzyme, assuming Vmax is 0.5M.sec-1 and the concentration of the enzyme used is 0.002M . why is it usefull to know this? 1.4) discuss the mechanism of the bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues. make use of relavant graphs and diagrams to explain your answer.Phosphoglycerate-mutase catalyses the isomerization of 3-phospho-glycerate to 2-phospho-glycerate. The enzyme has a molecular weight of 28,556 g/mol. In assays using 1 milligram of enzyme per assay the Km for 3-phosphoglycerate was 1.2 x 10^-3M and the Vmax was 840 μmole min^-1. What would be the approximate value of kcat (turnover number or molecular activity) of the enzyme under these conditions?Phosphoglycerate-mutase catalyses the isomerization of 3-phospho-glycerate to 2-phospho-glycerate. The enzyme has a molecular weight of 28,556 g/mol. In assays using 1 milligram of enzyme per assay the Km for 3-phosphoglycerate was 1.2 x 10^-3M and the Vmax was 840 μmole min^-1 or 14 x 10^-6 moles s^-1. What would be the approximate value of kcat (turnover number or molecular activity) of the enzyme under these conditions?