The following figure shows two absorption spectra. NAD* is the solid line. NADH is the dashed line.16NAD+12NADH240280320360Wavelength (nm)What is the wavelength of maximal absorbance of NADH in the 280-360 range?Molar absorbance x 103

To monitor the development of various enzymatic redox (oxidation-reduction) reactions, UV…

Answered: The following figure shows two…

Biomedical Instrumentation Systems

1st Edition

ISBN:9781133478294

Author:Chatterjee

Publisher:Chatterjee

Chapter6: Biomedical Electrodes, Sensors, And Transducers

Section: Chapter Questions

Problem 2P

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Refer to the figure shown here, and determine the value of E for the overall oxidation/reduction reaction (refer to the book/lecture slides if you need help with the overall reaction). 11/12102 + 2H* + 2e¯ → H₂0 NAD + H* + 2e → NADH O-1.136 volts 0.496 volts +1.136 volts -0.496 volts EU (volts) – 0.320
Refer to the figure shown here, and determine the value of E for the overall oxidation/reduction reaction (refer to the book/lecture slides if you need help with the overall reaction). 121/202 + 2H+ + 2e → H₂0 NAD + H* + 2e → NADH O-1.136 volts O 0.496 volts O+1.136 volts voltsm -0.496 volts EU (volts) +0.816 - 0.320
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).
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).
The glutamate dehydrogenase (GDH) catalyses the following reaction: *H₂N- H CH₂ CH₂ COO™ acide glutamique COO™ Time (min) A340 + NAD+ + H₂O The answer: GDH 2 1 1.760 1.718 [ammonium sulphate] = 0.33 M [NADH] = 0.205 mg.mL-¹ = 2.9.10-4 M [a-ketoglutarate] = 0.07 M [Protein] = 0.05 mg.mL-¹ COO™ CH₂ The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: 0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min Add 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start the reaction. 5 3 4 1.675 1.635 1.595 !- Calculate ammonium sulphate, NADH, concentrations in the reaction medium at t = 0. CH₂ The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data ENADH at 340 nm = 6220 M-¹.cm-¹ COO acide x-cétoglutarique O + NH4+ + NADH + H* 6 1.550…
explain in quantitative terms the circumstances under which the following reaction can porceed; L-malate + NAD+ (forward arrow) oxaloacetate + NADH + H+ delta G' standard = +29.7 KJ/mol
a) Calculate the enzyme and specific activity of a reaction with 3 pM 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 6200L 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
Perform the calculations to make a master mix for 20 1.0 mL reactions each composed of 165 uL of 6 mM NAD+ 165 uL of 0.15M Lactate and 630 uL of 0.15M CAPS pH 10.5 per reaction. Report your answers in units of milliliters.
Identify the oxidized and reduced forms of the following pairs: O2/H2O NO2- / NO3- NADP+ / NADPH FMN / FMNH2 α-ketoglutarate / isocitrate ___________________________________________________________________________ In photosynthesis, where in the chloroplast does the accumulation of protons occur as a result of the electron transport? Is this answer lumen of thylakoids?
Figure 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 Vmax
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
Acetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vmax) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 (S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (*"A JO %) A

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The following figure shows two absorption spectra. NAD* is the solid line. NADH is the dashed line. 16 NAD+ 12 NADH 240 280 320 360 Wavelength (nm) What is the wavelength of maximal absorbance of NADH in the 280-360 range? Molar absorbance x 103 4.