1 the concentration of the enzyme competition inhibitor was 1×10-3M. If 1 µmol of the inhibitor is present in the 1 mL reaction mixture, Indicate how much the initial degree of hydrolysis decreases as a proportion(in the presence of inhibitors/in the absence of inhibitors) with respect to the absence of inhibitors.
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1 the concentration of the enzyme competition inhibitor was 1×10-3M. If 1 µmol of the inhibitor is present in
the 1 mL reaction mixture, Indicate how much the initial degree of hydrolysis decreases as a proportion(in the
presence of inhibitors/in the absence of inhibitors) with respect to the absence of inhibitors.
Step by step
Solved in 2 steps
- Determine the Ki for the inhibitor at 30 °Cand decide what type of inhibitor is being used. Eo T I S V (g/I) (°C) (mmol/ml) (mmol/ml) (mmol/ml-min) 1.6 30 0.1 2.63 1.6 30 0.033 1.92 1.6 30 0.02 1.47 1.6 30 0.01 0.96 1.6 30 0.005 0.56 1.6 49.6 0.1 5.13 1.6 49.6 0.033 3.70 1.6 49.6 0.01 1.89 1.6 49.6 0.0067 1.43 1.6 49.6 0.005 1.11 0.92 30 0.1 1.64 0.92 30 0.02 0.90 0.92 30 0.01 0.58 0.92 30 0.6 0.1 1.33 0.92 30 0.6 0.033 0.80 0.92 30 0.6 0.02 0.57SUBSTRATE CONCENTRATION [S] µM INITIAL VELOCITY V0 s-1 10 0.13 25 0.27 50 0.45 100 0.65 150 0.77 200 0.85 300 0.94 500 1.03 (i) a) Construct an empty table with the following column headings: Substrate concentration [S] and initial velocity (Vi) where [S] has the unit µM, and Vi has the unit mM/s. (ii) The table provided is the enzyme kinetic data for your mutated enzyme, whereby Vi was expressed using the unit ∆A(405 nm)/s. Using the standard curve, express Vi with the unit mM/s rather than ∆A(405 nm)/s. Place your answer in the table above alongside the appropriate [S]. Hint: To answer this question you need to use this standard curve equation=0.0419x (The slope of the line is= 0.0419) (iii) The unmutated form of your protein has a Km of 25 µM and a Vmax of 43 mM/s. The enzyme kinetic data for your enzyme with the amino acid substitution should now be displayed in the table above. Based on these data, what is Vmax? Km? and…Fill up the two missing values inside the two circles knowing that the total reaction volume is 2mL. 1) Dilution fraction 2) Water Don't include units in your answer. Membrane Brillant blueR 1g/L Dilution Sample suspension fraction (μL) (μL) 1) Control ? 0 50 2) 1/200 ? 10 50 3) 1/100 0.01 20 50 4) 1/50 ? 40 50 5) 1/20 100 50 Phosphate pH11, 0.2M (ml) 1 1 1 1 1 Water (mL) 0.95 ? ? ?
- Rx Of oxacinophtalmic solution 3% Disp. 10 mL How many milligrams of axacin contained in each milliter of the dispensed prescription?Solution Absorbance mg/ml aspirin Standard solution - 1.6 mg/mL A 0.638 0.08 mg/mL B 0.504 0.064 mg/mL C 0.376 0.048 mg/mL D 0.259 0.032 mg/mL E 0.126 0.016 mg/mL A = -log T where T = %T ÷ 100 Construct a callibration curve using the above data. Absorbance should be on the vertical axis and "mg/mL of acetylsalicylic acid" on the horizontal axis. The line should go through the origin. Using the data provided, the graph you have generated, and the procedure that was used to generate the solutions which were examined by spectroscopy, calculate the amount of acetylsalicylic acid per tablet. Commercial tablet 1 labelled as 100 mg enteric coated Absorbance = 0.16 Commercial tablet 2 labelled as 300 mg Absorbance = 0.45 Student prepared tablet from practical 5 Absorbance = 0.19 Using the data provided, the graph you have generated, and the procedure that was used…a)Determine the amount of X (in gram) in order to prepare 100 mL of 50 mM stock solution of X. Show your work. (MW of X= 225) b)Determine the volume required (mL) from the stock solution X in (i) to prepare 500 mL of MS medium containing 5 mg/L X. Show your work.
- A 5% dextrose in 1/2 normal saline (D5 1/2 NS) solution is commonly administered to patients needing post-operative IV fluids. How could you prepare 500 mL of this solution? Dextrose is 5% (m/v) and the NaCl is 0.45% (m/v).The Ki for a competitive inhibitor pyrrole-2-carboxylate is 0.05M.Calculate the initial velocity if the substrate concentration is 0.25M and 1.0 mole/liter of the inhibitor is added to thereaction.Substrate Initial velocity Vo concentration [S] µM s-1 10 0.13 25 0.27 50 0.45 100 0.65 150 0.77 200 0.85 300 0.94 500 1.03 1. Calculate Vmax and Km??? The enzyme is dissolved at a concentration of 1 mg/ml and has a molecular weight of 50 kDa. a) What is the turnover number of the enzyme? b) What is the specificity constant of the enzyme? c) Is the enzyme operating near the maximum rate possible, i.e. is the enzyme diffusion controlled? please show all working and formulas as I am trying to learn. thank you
- How many moles are needed to prepare 95ml of 18%(mVmV) HCl ? molar mass HCl =36.45g/mol steps please3 mL of a 45 mM stock solution of a substrate is added to 8 mL of water. Calculate the following values. The substrate molecular weight is 125 g/mol. Calculate the following values: Substrate Volume in mL Dilution Factor Substrate number of moles Substrate concentration for the diluted solution in mM Substrate concentration for the diluted solution in mole/L Substrate concentration for the diluted solution in mg/mLTirofiban (C22H36N₂O5S MWt = 440.6) is present as tirofiban HCI monohydrate (C22H36N2O5S.HCI.H₂O MWt=495.1) at 0.281 mg/mL in a concentrated solution. A solution for infusion is prepared by extracting 50 mL from a 250 mL bag of 5% glucose solution and adding 50 mL of concentrated solution. Sofia who weighs weighs 87 kg requires a tirofiban dose of 0.1 mcg/kg/min for 12 to 24 hours. What would the infusion rate be (mL/h)? (Answer to 1 decimal place.) Answer: