Intestinal epithelial cells pump glucose into the cell against its concentration gradient using the Na-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 Na* ions into the cell to the "uphill" transport of glucose into the cell. If the Na* concentration outside the cell ([Na* Jou) 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. AGgloc= 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- 7.90

According to the “Hawaiian Punch” principle, different compartments of the secretory and endocytic pathways are topologically equivalent to each other and to the extracellular space. Explain how vesicular transport generates this topological equivalence. These compartments are topologically equivalent because molecules can move between them without having to move out of the cell. Transport vesicles cause this “topological equivalence” because they are responsible for the actual movement of the molecules mentioned above. They break off from one compartment, carrying the necessary molecules, and then fuse to its targeted compartment; thus, making the compartments topologically equivalent.  During mitosis in mammalian cells, the nuclear envelope breaks down into vesicles. Are the topological properties of the cell altered by this event? Justify your answer.

Is the movement of sodium through SGlut-1 during co-transport simple diffusion, facilitated diffusion, active transport, or secondary active transport? And is the movement of glucose through SGlut-1 during co-transport simple diffusion, facilitated diffusion, primary active transport, or secondary active transport?

a skeletal muscle cell has depleted its stores of ATP how will the altered transport properties of the NKA transporter affect cytosolic calcium concentrations (increase, decrease, no change) relative to normal? Why?

Compare the plots of the transport rates for both conditions. What is most likely mechanism of transport for serotonin into these cells? Explain your interpretation.

The uptake of l-ascorbate (vitamin C) and its oxidized form, dehydro-l-ascorbic acid (DHAA), was evaluated in brush border membrane vesicles isolated from adult human small intestine. Ascorbate uptake was Na+-dependent and potential-sensitive (Km, 200 umol/L), whereas DHAA transport occurred through Na+-independent facilitated diffusion (Km, 800 µmol/L). If the Vmax of vitamin C import through channels is 401µmol/min/cm2, what import rate would you expect if the lumen contained 133 µmol/L of the version of vitamin C that moves through them?

Our current experimental procedure works because Con A adheres strongly to the nitrocellulose membrane while HRP hardly binds to the membrane at all. If HRP binds as strongly to the membrane as Con A does, our current scheme will not work. Assuming that's the case (HRP strongly binds to the membrane non-specifically, regardless of the presence of ConA), you will need to treat the membrane with an additional solution before treating it with HRP. What solution would that be? O Saturated NaCI solution. O Concentrated HCI. A membrane-binding protein. Concentrated glucose slution.

A fixed amount of radiolabelled insulin was incubated with a fixed amount of anti-insulin antibody, the bound ligand was separated from free ligand at different time intervals. Draw a diagram of the concentration of the insulin/antibody complex with time. (Insulin/antibody complex is the bound ligand) asap typed only .

If you start with 100 mM Na+ and 100 mM K+ outside the liposomes, and 100 mM Na+ and 100 mM K+ inside the liposomes like in (A), then you add ATP to the solution outside the liposomes, then how will the Na+ and K+ concentrations change?

Two proteins bind to the same ligand with the following Kd's. Protein 1: 10 μΜProtein 2: 100 nM Which protein would be bound to more ligand at a ligand concentration of 10 μM? (Assume a limiting concentration of each protein)