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.
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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?
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- If a data from an enzyme experiment is plotted as a Lineweaver - Burk plot, and the Vmax is 0.02 sec/mol, and x-intercept is -2.5 mM-1, then what is the KM value?In the assay of citric acid, what do you think about the nature of solution sample ? a) Before titration and b) After titration.When you graph your protein assay data in Excel, should you include the absorbance of your unknown BSA sample? Explain why or why not
- What does an A280 of 0.000 indicate? What does this reading indicate in the context of your column chromatography? Are there still proteins adhering to the column? Do you know anything about the proteins which are still adhering to the column?In a gel filtration chromatography, what type of gel must be used when the protein size is 2500 Da? Explain.(a) The octapeptide AVGWRVKS was digested with the enzyme trypsin . Which method would be most appropriate for separating the products: ion-exchange or gelfiltration chromatography? Explain. (b) Suppose that the peptide was digested with chymotrypsin . What would be the optimal separation technique? Explain.
- First, they ran samples of the enzyme on denaturing and non-denaturing gels; the results are shown in the figure to the right. In addition, they ran the protein through a calibrated gel filtration column, the results of which indicated that the PYC enzyme had a molecular weight of 540 kiloDaltons. In the figure, the rightmost column are where molecular weight standards of various sizes would occur if they’d been on the gels. How many subunits are in the PYC enzyme? Are the subunits the same, or are they different in some way? Are the subunits made up of distinct chains of primary structures, and, if so, how many? Are the chains the same, or are they different in some way?) In urea assay (Catalog #K375-100) what is the nmol (range) it can detect?Consider the following properties of the protein components of a sample mixture as provided in the table below: 1. if the mixture is subjected to gel filtration chromotography which protein component elute first? 2. if the mixture is subjected to isoelectric focusing which protein will stop m oving nearest to the positive electrode? 3. if the mixture is subjected to cation-exchange chromotography using a buffer at ph 7 which protein will bind to the resin? 4.if the mixture is subjected to SDS-PAGE which protein will be at bottomost portion of gel? 5.if the mixture is subjected to hydrophobic interaction chromotography which protein will bind most strongly to the resin?
- What kind of techniques would be needed to take the structure properly taken into account in biochemical experiments?Which nuclear isotope used in protein NMR spectroscopy is the most sensitive to detect? Briefly explain why.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.