Answered: Determine Km, Vmax, and kcat (in 1/s)…

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?

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Which fractions measured from your gel filtration experiment had the most and least amount of protein detected? Which fraction likely contained the most myoglobin based off molecular weight and protein presence? Which fraction likely contained the most egg albumin based off molecular weight and protein presence? Which samples measured from your ion exchange experiment had the most protein detected? Calculate the approximate pI of your proteins using the ion exchange Table 2. Ion Exchange Samples Tested by Bradford Assay Concentration BSA (μg/mL) Concentration BSA (mg/mL) Volume of Sample added to Bradford Reagent (μL) Absorbance at 595 nm Standard 1 250 0.25 50 0.32 Standard 2 125 0.125 50 0.16 Standard 3 62.5 0.0625 50 0.08 Standard 4 31.25 0.03125 50 0.04 Standard 5 15.625 0.015625 50 0.02 Blank 0.00 0.00 0.00 Table 3. Gel Filtration Fractions Tested by Bradford Assay Fraction #:…
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.
i found this past paper however i cannot find the solutions, please can you answer question 1c
Lactose transporter of E. coli is a well-studied proton driven cotransporter. It transports one lactose molecule together with one proton into the cell. Calculate the free energy change for transporting one more of protons into the cell? Membrane potential is -50 mV (inside is negative) and the pH = 7.2 inside the cell and the pH = 4.0 outside the cell. Temperature is 37 degrees celsius (310K). Remeber to convert pH to (H+) and express your answer as kJ/mol.
Covid-19 patients may develop acute pulmonary edema (fluid retention in the lungs), and furosemide is often used to treat it. Another potential complication of covid-19 is acute kidney damage. Possible causes include hypoxia, blood clots and inflammation. To evaluate a patient for kidney damage, a medical team took blood samples and placed a catheter to collect urine for 24 hrs. Here are some results: Plasma creatinine: 50 mg/100 mL plasma Urine creatinine: 40.8 mg/mL urine Urine production: 1.5 L in 24 hr 1. What was the patient's creatinine clearance in mL/min? (Creatinine clearance = excretion rate of creatinine/plasma concentration creatinine). Show your work.
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What is an Hfr cell? How does it differ from F-, F+, and F-? What is the definition of an exconjugant in relation to this?
(e) Two ADP agonists (drugs) were also found to bind to platelets: 2-methylthio-ADP bound with a Kp of 7 µM and 2-(3-aminopropylthio)-ADP bound with a Kp of 200 µM. Can these drugs effectively compete with ADP for binding to platelets? Explain your answer.
PTP1B Substrate kcat Km kcat/Km UM 10-7 x (s-1 M) DADEPYLIPQQG DADAPYLIPQQG DAAEPYLIPQQG AAAAPYLIPQQG 44.6 + 1.8 39.8 + 0.32 3.9 + 0.9 13.7 + 0.46 1.1 + 0.25 0.29 + 0.01 35.3 + 0.22 6.6 ± 0.22 0.53 + 0.02 34.7 + 0.25 52.7 ± 0.7 0.066 + 0.001 (d) (. ) The units for kcat/KM in the above are given according to standard scientific notation. On this basis what is the value of this kinetic parameter for the DADEPYLIPQQG substrate?
From experiments in which cells expressing normal myosin II heavy chain were altered to either lack (mhckA-) or overexpress (MHCKA ++) a myosin heavy chain kinase (MHCKA). For answering this question recall the earlier the variants on the myosin II heavy chain, in which three key threonines, normally subject to reversible phosphorylation, were altered in various ways: 3X Ser = Serines in place of Threonines 3X Ala = Alanines in place of Threonines 3X Asp = Aspartate in place of Threonines MHCKA is present at normal levels. Which of the two mutants (mhcp- or MHCP++) would be most likely to have a defect in cytokinesis?
In your own words, briefly describe the function of FeSO4 in the KIA medium in one sentence.