1. Consider the following set of data and answer the following questions: IS) (M) 6x 10 1x 105 2x 105 6x 105 1.8 x 10 V (umol/min) V (+ Inhibitor) (umol/min) 20.8 12 29 15 45 20 67.6 24 87 28 a. Plot the data on a Lineweaver-Burk plot (be sure to label axes) b. Determine the Km C. Determine the Vmax d. The second set of velocities represents the rate of the reaction when an inhibitor is added. Plot these data on the same graph as above and detemine the new Km and Vmax and the type of inhibitor (competitive, uncompetitive, non-competitive). e. Can the effects of the inhibitor be over-ridden by adding more substrate? Why?
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Consider the following set of data and answer the fo
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- 4. A physician orders an IV drip containing 12 million units per day of penicillin G potassium for a patient with otitis media (middle ear infection). A. If 18.2 mL of diluent is used to reconstitute the penicillin G, how many mL should be injected? B. If 8.2 mL of diluent is used to reconstitute the penicillin G, how many mL should be injected? C. If 3.2 mL of diluent is used to reconstitute the penicillin G, how many mL should be injected?Using the substrate Ac-Ser-Gln-Asn-Tyr*Pro-Val-Val-NH2 and 10 nM HIV-1 protease, an inhibitor showed competitive inhibition, and a family of lines of 1/v vs. 1/[substrate] at changing-fixed concentrations of this inhibitor were as below: Slope (apparent Km/Vmax) (sec): 17,241 21,072 24,904 28,735 32,567 [Inhibitor] (M): 0 10 20 30 40 The Ki value for this inhibitor is _________________1. How many TSS sites were identified using this technique? 2. Look at the labels next to each of the annotated TSSs. What are the labels for the TSS sites? 3. What is the coordinate for TSS_tra_16584216?
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- 1.a)What is the equivalence point and how does it relate to the recommended proportion of serum to blood in the heme agglutination assay? b. what would the predicted outcome be if you used too little serum in this assay? Why? c. what would the predicted outcome be if you used too much serum in assay? Why?(b) Both laboratories used 10 micrograms of protein each in their kinetic assays. Protein concentrations weredetermined by the Bradford protein assay. Assay conditions employed in the two labs (pH, temperature,etc.) were also identical. What would be the most plausible cause for the discrepancy in the Vmax valuesfor the compound I? Explain.Recall that the Bradford assay measures total protein amounts in sample solution based on complexformation between a dye and proteins. Also, the assay solution used in both labs does not contain anyinhibitors.The following assays is/are considered a DIRECT ASSAY: A. absorbance B. рн C. Viscosity D. All of the above Which of the following is/ are statement/s NOT describing enzyme activity? A. Activity is inversely proportional to the concentration B. It is a reflection of its concentration C. It is commonly measured in terms of their catalytic activity D. None of the above What is the difference between enzymes from antibodies? A. ability to bind with compounds with great specificity and high affinity B. bind in high energy state C. binds the complementary structure in its ground state D. All of the above
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