Intestinal epithelial cells pump glucose into the cell against its concentration gradient using the Na-glucose symporter. Recall that the Na+ concentration is significantly higher outside the cell than inside the cell. The symporter couples the "downhill" transport of two Na+ ions into the cell to the "uphill" transport of glucose into the cell. If the Na+ concentration outside the cell ([Na+ lout) is 155 mM and that inside the cell ([Na+ lin) is 21.0 mm, and the cell potential is -52.0 mV (inside negative), calculate the maximum energy available for pumping a mole of glucose into the cell. Assume the temperature is 37 °C. AGgluc = kJ mol What is the maximum ratio of [glucose]in to [glucose]out that could theoretically be produced if the energy coupling were 100% efficient? 2700 7.89 1.14 3.7 x 10-4
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- Intestinal epithelial cells pump glucose into the cell against its concentration gradient using the Na+– glucose symporter. Recall that the Na+ concentration is significantly higher outside the cell than inside the cell. The symporter couples the "downhill" transport of two Na+ ions into the cell to the "uphill" transport of glucose into the cell. If the Na+ concentration outside the cell ([Na+]out) is 163 mM and that inside the cell ([Na+]in) is 21.0 mM, and the cell potential is −54.0 mV (inside negative), calculate the maximum energy available for pumping a mole of glucose into the cell. Assume the temperature is 37 °C.Intestinal epithelial cells pump glucose into the cell against its concentration gradient using the Na-glucose symporter. Recall that the Na* concentration is significantly higher outside the cell than inside the cell. The symporter couples the "downhill" transport of two Na* ions into the cell to the "uphill" transport of glucose into the cell. If the Nat concentration outside the cell ([Na lout) is 141 mM and that inside the cell ([Na* lin) is 19.0 mM, and the cell potential is -52.0 mV (inside negative), calculate the maximum energy available for pumping a mole of glucose into the cell. Assume the temperature is 37 °C. AGglac 9.63 Incorrect kJ mol What is the maximum ratio of [glucose), to [glucose)out that could theoretically be produced if the energy coupling were 100% efficient? O 2700 1.13 3.7 x 10- 7.90Calculate the membrane potential in the transport of Cl- from the intracellular environment to the extracellular environment. The Cl- concentration outside the cell is 98 uM, the Cl- concentration in the cytoplasm is 0.025 mM, the Gibbs free energy is -956 J/mol and the temp is 37°C. Have concentration in uM units when solving.
- The following table shows experimental results of the glucose transport rate, mM/sec, following facilitated diffusion by glucose carrier proteins. (Recall: the starting conc. L represents glucose added to one side of the membrane; distilled water, omM of glucose was added to the other side of the membrane). The rate of glucose transport was 0.0031 mm/sec with 8mM of glucose (run number 4, highlighted); the rate decreased to 0.0017 mM/sec with 10mM of glucose (run 5, highlighted). Why was the rate of glucose transport slower when the concentration gradient was increased? Experiment Results Run Number Solute 1 1 2 2 3 33 4 4 5 6 6 Na Ch Glucose Na Ch Glucose Na Ch Glucose Nat Ch Glucose Na Ch Glucose Nat Cl Glucose Start Conc. L Start Conc. R (MM) (mM) 0.00 0.00 2.00 0.00 0.00 0.00 8.00 0.00 0.00 0.00 2.00 0.00 0.00 0.00 8.00 0.00 0.00 0.00 10.00 0.00 2.00 0.00 2.00 0.00 Carriers 500 500 500 500 700 700 700 700 100 100 700 700 Rate (mm/sec) 0.0000 0.0008 0.0000 0.0023 0.0000 0.0010…O Att Intestinal epithelial cells pump glucose into the cell against its concentration gradient using the Nat-glucose symporter. Recall that the Nat concentration is significantly higher outside the cell than inside the cell. The symporter couples the "downhill" transport of two Nat ions into the cell to the "uphill" transport of glucose into the cell. If the Nat concentration outside the cell ([Na lout) is 161 mM and that inside the cell ([Na* Jm) is 17.0 mM, and the cell potential is -50.0 mV (inside negative), calculate the maximum energy available for pumping a mole of glucose into the cell. Assume the temperature is 37 °C. What is the maximum ratio of (glucose] to [glucoselout 10.62 kJ AG gluc mol that could theoretically be produced if the energy Incorrect coupling were 100% efficient? O 1.13 8.24 3800 2.6 x 10 IncorrectTHOUGHT QUESTION Imagine we identify a gene that is directly responsible for the effects of vasopressin on male mammals, including humans-we will call it trust1-that leads to the production of a vasopressin receptor in the brain, which we will call TRUST1. There are different versions of trust1, all of which lead to different levels of the behavior associated with this neuropeptide on male behavior. Give some examples where it would be a good idea to know a particular males genotype-that is, which of the trust1 genes he has. Give an example of when you think science has gone too far and this information should not be known.
- Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Calculate the Km of the reaction represented by Line (B).Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Calculate the catalytic efficiency of the reaction represented by Line (A).Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Line (B) represents ____________. A. an enzyme-catalyzed reaction in the absence of any inhibitor. B. an enzyme-catalyzed reaction in the presence of a competitive inhibitor. C. an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor. D. an enzyme-catalyzed reaction in the presence of a noncompetitive, or mixed, inhibitor.
- Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Calculate the Vmax of the reaction represented by Line (C). Show all mathematical work, please.Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. QUESTION: Line (A) represents ____________. A. an enzyme-catalyzed reaction in the absence of any inhibitor. B. an enzyme-catalyzed reaction in the presence of a competitive inhibitor. C. an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor. D. an enzyme-catalyzed reaction in the presence of a noncompetitive, or mixed, inhibitor.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)?