Calculate the osmotic concentration of a solution consisting of 33.15 g NAD (C21H27N7014P2; mw = 663 g/mol) and 15.72 g FAD(C27H33N9O15P2; mw = 786 g/mol) in 100g of water.
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- 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…Incubating 10µl of an LDH sample for 5 min in the presence of 60mM of lactate and 100mM NAD+ resulted in an OD = 1.2. Total volume is 1ml. The protein 340nm concentration of the LDH sample was 2000µg/ml. Calculate specific activity in U/µg of protein (1 Unit of enzyme catalyzes the conversion of 1 µmole of substrate to product.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).
- (b) the activity of the malate-aspartate shuttle (MAS) system of isolated rat brain mitochondria suspended in an isotonic me- dium buffered to pH 7.4. Diagram A illustrates NADH fluo- rescence emission upon addition of Glutamate in the ab- sence and presence of Aspartate. Diagram B illustrates sim- ilarly NADH fluorescence emission upon addition of Gluta- mate in the presence of Aspartate followed by additions of submicromolar concentrations of Ca2+. As is well estab- lished, the MAS in brain, skeletal muscle, and cardiac mus- Diagrams A and B on the right show changes in Glu A Glu В -No Asp + 0 +0.12 -0.48 + 16 0.81 +1.8 ++ Asp 10 min 2 min cle mitochondria is activated by cytosolic concentrations of Ca2* < 3 µM. To simulate the cytosolic part of the MAS, the following reagents were added to the medium: 4 units/ml glutamate-oxaloacetate transaminase, 6 units/ml malate dehydrogenase, 66 µM NADH, 5 mM aspartate, 5 mM malate, 0.5 mM ADP, 200 nM ruthenium red (to block the mitochondrial…Carbonic anhydrase catalyzes the hydration of CO. CO2 + H2O ¬ H½CO3 The Km of this enzyme for CO, is 1.20×104 µ.M. When [CO,] = 3.60×104 µM, the rate of reaction was 4.50 umol·mL! sec-1 a What is Vmax for this enzyme? umol·mL-!sec-!Study is being done where protein A isomerase (AI) is being phosphorylated by AI phosphorylase (AIP), at 37oC at physiological pH of approximately 7.4 with excess of Mg2+ and ATP. The Vmax and Km are determined to be 9 mM s-1 and 15 uM, respectively a) does AIP need any coenzymes, cofactors, co-substrates? b) what would be the formula for initial rate as a function of AI concentration? (Michaelis-Menten equation) c) what are the intial rates of reaction when [AI] = 3, 6 and 40 uM? Is the trend in initial rate vs [substrate] surprising? Explain.
- In considering active transport by Na + -K + -ATPase at body temperature (37 o C), 3 Na+ are pumped out of the cell and 2 K + are pumped in for each ATP that is hydrolyzed to ADP + P i . Given that underyour experimental conditions, the DG for ATP hydrolysis is -10 kcal/mol, and that V is -60 mV, and that the pump maintains the internal Na + at 10mM, external Na + at 120 mM, internal K + at 120 mM and external K + at 8mM, what is the efficiency of the pump (i.e., what fraction of the energy available from ATP hydrolysis is required to drive transport at the provided levels)?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) aboveKt of glucose for GLUT1=3 mM, GLUT2=17 mM, GLUT 3=1.3 mM, and GLUT11=0.3 mM. Sketch a graph with [glucose] on the x-axis and rate of transport on the y-axis. Sketch a line for each GLUT transporter above. Which of these GLUT transporters will be working at its maximum rate at [glucose]=5 mM? Which of these GLUT transporters will be working closest to ½ Vmaxwhen [glucose]=5 mM? What will be the approximate rate of glucose transport for each of these transporters if [glucose]=17 mM?
- During vigorous exercise, a buffer system consisting of lactic acid and sodium lactate is produced in the muscle cells and released into circulation. (a) Calculate the concentration of lactate in the blood plasma (pH= 7.40) if the concentration of lactic acid in the blood is 1.50µM. {The pKa for lactic acid is 4.76}. (b) How is NADH recycled to NAD+when oxygen is a limiting factor during vigorous exercise? (c) Indicate the biochemical transformation that occurs in (b) above when aerobic conditions are restored during the resting state.The drug troglitazone was used to treat diabetes but was withdrawn from the market when patientswho took the drug suffered from severe side effects. The data below show the activity of an enzymein the steroid biosynthetic pathway in the presence and absence of 10 µM troglitazone.[S] (µM) v0 (pmol min-1)Create a plot of 1/v0 vs. 1/[S]. Calculate KM and vmax in presence and absence of inhibitor. Whattype of inhibitor is troglitazone? Clearly support your answer.Calculate glucose concentration. Na (sodium) and glucose secondary active transport. Na transport (which drive glucose import) G=R*T*In(Na in/ Na out)+Z*F*Y(psi symbol) Na in=14mM Na out=145MM Z=+1 F=96.5 KJ/V*mol Y(psi)=-0.05V What is the glucose in and out concentration? Please be very through when explaining this calculation. (I am stuck at why the energy sign changes from negative to positive when using the calculated energy from sodium to glucose)