Why was absorbance measured at 420 nm in the enzyme kinetics experiment? To monitor the
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pls explain
Why was absorbance measured at 420 nm in the enzyme kinetics experiment? To
monitor the
a. decrease in catechol concentration
b. increase in quinone concentration
c. decrease in polyphenol oxidase concentration
d. polyphenol oxidase-catechol complex concentration
Lineweaver-Burk plot is the most used linearization method of the MichaelisMenten equation, but the main drawback is a/an:
a. overemphasis to low substrate concentration and less emphasis to high
substrate concentration.
b. overemphasis to high substrate concentration and less emphasis to low
substrate concentration.
c. exaggeration to both ends of the reciprocal of the substrate concentration.
d. lack of independent variables to x- and y- coordinates
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- a) Determine kcat (in units of sec-1) for a particular enzyme, given the following information: Vo = 144 mmol/min; [S] = 2 mM; Km = 0.5 mM; Enzyme Molecular weight = 40,000 mg/mmole; 8 mg of enzyme used in assay generating this data. b) In general, explain how the total enzyme concentration affects turnover number and Vmax?Let’s consider vmax. Recall that uncompetitive inhibitors bind to the enzyme only after thesubstate is bound.a) As the concentration of substrate increases, the fraction of enzyme bound to substrate (circleone) increases / decreases?b) Does an uncompetitive inhibitor bind more readily when the substrate concentration is low orhigh?1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?
- MATHEMATICAL The enzyme -methylaspartase catalyzes the deamination of -methylaspartate [V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)]. The rate of the reaction was determined by monitoring the absorbance of the product at 240 nm(A240). From the data in the following table, determine KM for the reaction. How does the method of calculation differ from that in Questions 26 and 27?MATHEMATICAL You do an enzyme kinetic experiment and calculate a Vmax of 100 mol of product per minute. If each assay used 0.1 mL of an enzyme solution that had a concentration of 0.2 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol?Calculate α' for an inhibitor with KI' = 10.0 nmol L-1 when 100 nmol L-1 of inhibitor is present.
- 1. Can the absorbance readings be used as a measure of enzyme activity atdifferent pH’s? 2. Describe an industrial application in which control of temperature and pHare critical to optimal enzymatic function.Enzyme X has a molecular weight of 48,000. It converts substrate Z into product Y. Z absorbs at 340 nm, and Y absorbs at 480 nm. A.) At what wavelength would you measure the change in absorbance to assay for enzyme X? Would the absorbance increase or decrease over time? B.)If Vmax = 60 μmol/min and you used 400 μL of a 0.1 mg/mL solution of enzyme, what is the turnover number?Protein concentration can readily be determined using the Beer-Lambert law: A = e l c where A = absorbance e = molar absorption coefficient (M-1cm-1) l = light path length (cm) c = concentration (M) If the molar absorption coefficient at 280 nm for yeast ADH is 48860 M-1cm-1 and a 10 mL solution of the protein has an absorbance at 280 nm of 0.4 (as measured by a spectrometer with pathlength 1 cm), then what is the concentration of the protein solution (in μM)? i.e. concentration = ______ μM If the molecular weight of the protein is 36849, what is its concentration in mg/mL? i.e. concentration = _______ mg/mL For each part of the question, show your calculations to arrive at your answers.
- Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…4. a. Calculate the KM (Michaelis constant) and the vmax (the maximum initial rate) for both substrates (sphingosine and ATP). Show your work, and be careful about units. b. threo-dihydrosphingosine, a stereoisomer of sphingosine, is an inhibitor of sphingosine kinase. What kind of inhibitor (competitive, uncompetitive, noncompetitive) is threo-dihydrosphingosine? Citing information from the Lineweaver-Burke plots, explain how you can tell.How can you find Kcat if you are only given Vmax, Km and [E] ? I tried using Kcat=Vmax/[E] but that didn't work. How do you know if [E] is the same as [E]total, and if it isn't how do you find it from this information: The Vmax for a particular enzyme is 10 nmols/L/s. The Km for its substrate is 5 microM. If the enzyme concentration is 10 nM, what is the kcat? a.80 nmoles/L/s b.8000 nmoles/L/s c.2 nmoles/L/s d.50 nmoles/L/s
