Please calculate the ΔG of glucose transport into the cell if the concentration of glucose is 1mM inside the cell and 100μM outside. R=2cal/mol*K and T = 300K. A. 1.38kcal/mol B. -1.38kcal/mol C. 2.76kcal/mol D. -2.76kcal/mol
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Please calculate the ΔG of glucose transport into the cell if the concentration of glucose is 1mM inside the cell and 100μM outside. R=2cal/mol*K and T = 300K.
A. 1.38kcal/mol
B. -1.38kcal/mol
C. 2.76kcal/mol
D. -2.76kcal/mol
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- 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)Calculate all the glucose data into cmol. What is the number of cmol glucose at timepont 10.42 (19.65 g/L)?What is the Keq for the conversion of Glucose 6-Phosphate to Glucose 1-Phosphate if the phosphate transfer potential for Glucose 1-Phosphate and Glucose 6-Phosphate are -20.9 kJ/mol and -13.8 kJ/mol respectively? Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a 0.27 b 0.45 c 10.5 d 0.019 e 0.057 f 24.2 g 7.10 h 0.24 i 2477
- A.What is the Result of the sodium potassium ATPase activity in the cell? B.What mechanism does the sodium potassium ATPase use to achieve this result? C. Why is the above-mentioned change in affinity critical for the sodium potassium ATPase to perform its function?It takes 9.4 msec for Enzyme X to catalyse a single reaction when it is fully saturated with substrate. Calculate the Vmax of the reaction if the concentration of Enzyme X is 2.4 mM. Select one: a. 26 mM/sec X b. 3.9/sec c. 0.26 M/sec d. 0.039 M/sec e. 106.4 M/sec13. 0.9% (m/v) NaCI solution and 5% (m/v) glucose solution are both isotonic to red blood cells. SHOW your work and watch sig figs & units. c. convert the concentration from M to % (m/v) for a 0.342 M NaC solution. (HINT: convert to g/ml and then multiple by 100%)
- Calculate the free energy change for glucose entry into cells when the extracellular concentration is 4.5 mM and the intracellular concentration is 2.1 mM at 37oC. Express your answer in kJ/mol.Calculate the Vmax of the above enzyme (lactase). (the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM) 0.125 mM per minute 0.25 mM per minute 0.50 mM per minute 1.25 mM per minute 5.0 mM per minuteAcetazolamide 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
- 1. The diagram below plots the free energy of glycolytic intermediates in mature red blood cells. +10 AG°' = - 130.9 kJ AGU -10 AGO 130 9 kJ (-31.3 kcal) or -20 - 31.3 kcal -30 -40 AG = AG 103.8 KJ (-24.6kcal) -50 AG 103.8 kJ -60 or - 24.6 kcal -70 GLU G6P F6P FBP GAP GBP PG3 PG2 PEP PYR LAC Note that Gor free energy in kcal is indicated along the vertical axis. The abbreviations in upper case letters along the horizontal axis at the bottom represent the various intermediates in the glycolytic conversion of glucose to pyruvate and to lactate. Therefore, the difference in any two points on the graph represents the difference in free energy between the two points. For instance, the AG'and the AG indicated with arrows on the left-hand end of the graph represent the two types of free energy changes associated with the conversion of glucose to glucose-6-phosphate catalyzed by hexokinase. bB S dD, write the equation (a) showing the relationship of AG and AG°' with respect to the mass-action…Calculate delta G of glucose transport into the cell if the concentration of clugoce is 1mM inside the cell and 100uM outside. R=2cal/mol*K and T=300KAcetazolamide 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 Vma) 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. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide. Sketch a graph of V versus [S] showing curves in the absence of an inhibitor and in the presence of the types of inhibitors not shown by acetazolamide. ("AJO %) A