oa obtain tne following data for the uptake of leucine and valine inside the cell with and without Na" ions present. Presence of Na+ V max Absence of Na+ Kt Substrate Vmax L-leucine 420 0.24 23 0.20 D-leucine 310 4.7 5 4.7 L-valine 225 0.31 19 0.31 (b) Which substrate seems to be preferred (binds better, or is more efficient) by the transporter? Explain your choice. (c) Draw a simple diagram and show whether this data suggests if the transporter is a symporter, antiporter, or uniporter of leucine and Na*.
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- CYP2E1 has a much higher Km for ethanol than ADH (11 mM versus 0.05 mM,respectively). When greater portions of ethanol are ingested (0.08% or 17 mM), which part of the statement would be true?Determine Km, Vmax, and kcat (in 1/s) for VF-6-2 efflux out of vesicles made from DV membranes with wild type PfCRT. What does the mutation in PfCRT appear to do to transport of VF-6?Based on your Lineweaver-Burk plot, what is the mode of PaESBL-1 inhibition by NSAMB? What is the equation for the double-reciprocal plot at 20 nMnM NAMB?
- The GadC anti porter also transports the amino acid glutamine(Gln). Do you think this activity has any role to play in combating low ph environments? How would you test this hypothesis?Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minuteA protein (PrX) was heated in vitro to 45C for 15 min, in the presence or absence of Hsp40, Hsc70, and ATP. The amount of PrX in aggregated (P, pellet) and soluble (S) fractions was then quantified (Bars, 1 SD). Based on these data, answer the following questions. In all cases, give brief justification for your answer. a) How does Hsp40 alone influence the solubility of PrX? b) How does Hsc70 alone influence the solubility of PrX? c) Do Hsp40 and Hsc70 co-operate in this experiment? d) Which components combined provide maximal solubility of PrX after heat shock?
- ) Dr Merrick is so excited to know the affinity constant Kd values for O2 binding to mammoth OBP and elephant hemoglobin at pH=7, that he starts speculating about the kinetics of binding to O2. If the ka value of mammoth EHb-O2 complex was the same as the ka value of mammoth OBP-O2 complex, what would be the ratio between the kd values of these complexes? Explain your reasoning. Hint: we are looking for the ratio kd(EHb)/kd(OBP) at pH=7.Calculate the mass of invertase (in mg) and concentration of invertase (in mM) contained in a 25.0mL sample of yeast extract that has 3,000 total units of activity, assuming that pure invertase has a specific activity of 1,000 units/mg with a mass of 270kD.Hypothetical scenerio: When the membrane potential is 80mV across the digestive vacuoles (DV), inside positive, the Vmax for VF-6-2 efflux is 15pmol/h. However, when the membrane potential is 80mV inside negative, the Vmax of VF-6-2 efflux drops to near zero. Researchers suggest an H+ P-type ATPase is also in the membrane and is required for VF-6-2 efflux. Do these data support their suggestion? What type of transporter might PfCRT be? How can vanadate be used to potentially test their idea?
- Approximate P50 for myoglobin from its binding curve. Approximate P50 for normal hemoglobin and the hemoglobin mutant from the binding curve. At low pO2 (below 20 Torr), which binds O2 with greater affinity, normal hemoglobin or the hemoglobin mutant? At high pO2 (above 30 Torr), which binds O2 with greater affinity, normal hemoglobin or the hemoglobin mutant? Which protein, normal hemoglobin or the hemoglobin mutant, transports O2 more efficiently? Briefly explain your answer.a protein collected through affinity chromatography displays no activity even though it is found to have a high concentration using the bradford protein essay. what best explains these findings?In chymotrypsin, a mutant was constructed with Ser 189, which is in the bottom of the substrate specificity pocket, changed to Asp. What effect would you predict for this Ser 198 → Asp 189 mutation? Explain your answer.