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- 1. Write down the identification reactions for lodine. Specify the reaction conditions.For the reaction 2Na (g) Na2 (g) the following values of K have been determined (C. T. Ewinget al., J. Chem. Phys. 1967, 71, 473):T (K) K900 1.321000 0.471100 0.211200 0.10From these data, estimate rxnH° for the reaction.A penicillinase inactivates a penicillin. An enzyme with Mw = 30,000 has only a single active site, kcat = 2,000 s-1 and KM = 5.10-5 M. In response to a treatment with 5 μmol of penicillin, a 1 mL suspension of bacteria releases 0, 5 µg of enzyme. A) What concentration of penicillin would cause the enzyme to react at half the maximum rate? B) A modified penicillin acts as a competitive inhibitor. If the affinity of E for penicillin and for modified penicillin are the same, what concentration of inhibitor reduces the rate of penicillin loss 5-fold with low Cs in the medium?
- A protein catalyzes the following reaction and had a Michaelis-Menten constant of Km=25 mM and a turnover number of 4.0 x 107 s-1. The total enzyme concentration is 0.012 µM and the initial substrate concentration is 4.76 µM. The enzyme has a single active site. Calculate the values of Vmax and V0 for this enzyme. 2H2O2 (aq) -----> 2H2O(l) + O2(g) Vmax= Vo=Trypsin is a serine protease that has a KM of 15 mM. At an initial substrate concentration of 250 µM insulin, trypsin is found to degrade insulin at a rate of 0.6 µM/min. If the concentration of trypsin in solution was 4.326 µM, what is the kcat of trypsin in s-1?explain why? • Levofloxacin is a broad spectrum antibotic. It is reported that itis completely removed in an unchanged from the body and itselimination half life is 7 h. Determine the amount oflevofloxacin eliminated in urine at 10 h following IV bolusadministration of 6,25 mg/kg dose to a patient weighing 80 kg.a. 185,75 mgb. 314,25 mgc. 314,25 mg/kgd. 18,57 mg How long will it take to lose 75% of the administered doseof a drug from the body if the drug follows first orderprocess?a. 3,32 half livesb. 2,32 half livesc. 2.0 half livesd. None of the above
- 23a, no need to explain too muchAcetylcholinesterase is an enzyme that catalyses the hydrolysis of acetylcholine to choline. After several purification methods, 44.0 µg of acetylcholinesterase was purified from a crude extract and was found to catalyse the conversion of 16.0 μmol of acetylcholine (the substrate) to choline (the product) in 9 mins. What is the specific activity of acetylcholinesterase in units μmol min-1 mg-1. (Round your answer to the nearest whole number. (i.e. If you calculated 40.03, input your answer as 40. Input only the numerical value. Do not input the unit).For the reduction 2FeCl3 + SnCl2 =====➔ 2 FeCl2 + SnCl4 in aqueous solution the following data were obtained at 25oC t(min) 1 3 7 11 40 Y 0.01434 0.02664 0.03612 0.04102 0.05058 Where y is the amount of FeCl3 reacted in moles per liter. The initial concentrations of SnCl3 and FeCl3 were respectively, 0.03125, 0.0625 moles/L. a.)Show that the reaction is third order (derive the rate law), and b.) calculate the average specific rate constant.
- The kinetics of an enzyme are measured as a function of [S] in the presence and absence of 2 mM I. Compute Km and Vmax in the absence and presence of I S] (uM) V (uM/min) without I with I 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8The equilibrium constant for the attachment of a substrate to the active site of an enzyme was measured as 200. In a separate experiment, the rate constant for the secondorder attachment was found to be 1.5 x 108 dm3 mol-1 s- 1. What is the rate constant for the loss of the unreacted substratefrom the active site?Dr. Alghe has just performed a restriction digest on DNA she extracted from her samples. She must now run her DNA out on a gel to separate the fragments based on size. To do this she must prepare a 1.2% agarose gel, where the percentage is determined as mass/vol. How many grams of agarose must she add to 200 mL of buffer in order to arrive at the correct percentage?