After calculating the extinction coefficient for lysozyme above, you convert it intoml mg cm1 units. (You need not do the calculation, just suppose you did).To calculate the protein concentration in your column fractions (W1-3, E1-2), wouldyour calculated extinction coefficient be a better choice than 1.5 mL mg 1 cm1 valuelisted in the theory section of your pre-lab? Why or why not?(Choose the best response)Yes, because we expect all of the column fractions to be mainly lysozyme.No, because most, if not all, the column fractions are mixtures of 2 or moreproteins.Trick question, we should use the values calculated by EXPASY for lysozyme.Yes, because my calculated value is more accurate than values from theliterature.ONo, because lysozyme is still stuck to the column and shouldnot be in any of ourcolumn fractions.

Lysozyme is a low molecular weight enzyme (~14kDa), it hydrolyzed the beta-1,4 linkage between…

Answered: After calculating the extinction…

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 of the following is NOT a unit of concentration? All of these options are units of concentration. mM Moles/Liter Molar You gathered your data from Lab , and found the following values: Total Activity of lysozyme in HEW: 14 units Total Activity of lysozyme in carb 1: 21 units Total amount of protein in HEW: 70 mg Total amount of protein in Carb 1: 15 mg Calculate the extent of purification of lysozyme in Carb 1. A 7 fold B 150% C 15 fold D 70%
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?
Explain in details how you could separate a mixture of three amino acids Arg, Lys, and Cys using ion-exchange chromatography. For the toolbar, press ALT F10 (PC) or ALT+FN+F10 (Mac). ...
Four proteins Cytochrome C (pI=10.2) Myoglobin (pI=7.2), Hemoglobin (pI = 6.8) and Serum Albumin (pI= 4.8) were used in our gel electrophoresis lab exercise. If the electrophoretic separation is carried out at pH 7.0, which protein would move toward the negative electrode? Cytochrome C Myoglobin Hemoglobin
A spheroidal bacterium with a diameter of 1.0 mm (micrometer, 1 mm = 10-6) contains 25,000 molecules of the protein hexokinase. What is the molar concentration of the protein inside the cell?
What is the expected outcome of the ion exchange chromatography using lysozyme as outlined above? Will the protein be separated successfully or not using the materials stated in the above? Provide a brief explanation to your reasoning please answer correctly, not written assigment
The A280 of a protein sample loaded onto a gel was determined to be 0.767 (1.00 cm path length, after subtracting the blank). The total volume of this sample was 428 µL. 19.0 µL of this protein sample was mixed with 19.0 µL of 2X laemalli sample buffer and then 12.0 µL of the entire sample was loaded into the gel and electrophoresed. Calculate the amount of protein that was loaded into the gel (in µg).
This SDS-PAGE loading buffer has SDS (a denaturing detergent), β-mercaptoethanol (a reducing agent), Coomassie Blue (a dye), and glycerol. You will need to dilute your protein samples such that the final concentration of the loading buffer is 1x, meaning that you will add 5 parts of the protein sample for every 1 part of 6x buffer. Calculate how much of the 6x loading buffer you will need to add to each sample. Then, add the appropriate amount of 6x SDS-PAGE loading buffer to the samples. Store the samples in the -20°C freezer. What is the final concentration of glycerol in each of the samples?
Consider the following protein mixture: Protein A B C D Molecular Weight (kDa) 50 150 200 350 Affinity to Metal ion === Zn²+ === 1. Using hydrophobic interaction chromatography, the protein that will be eluted last is [Select] 2. Using affinity chromatography, the protein that will be eluted last in a Zn²+-containing column is 3. The protein with the fastest migration towards the anode in SDS-PAGE is [Select] IpH value 7 3 9 5 [Select] [Select] 4. Using a buffer solution with a pH of 4, the protein that will bind to an anion exchanger is 5. The protein that will be eluted last in a gel filtration column is [Select] 6. Using isoelectric focusing, the protein that will have a protein band nearest to the cathode (negative electrode) is [Select] % Hydrophobicity 20 45 75 55
A series of standard proteins and an unknown enzyme were studied by gel filtration on a Sephadex G200 (the 200 refers to the maximum pore size in kDa) column. The elution volume Vel for each protein is given in Table 1 below. (a) Plot the data in the form of log Mr versus elution volume. From the line of best fit through the points for the standards, determine the Mr of the unknown enzyme. Explain why ferritin and ovomucoid behave anomalously. Table 1 - The Vel versus Mr data Protein Mr Vel (mL) Blue dextran* Lysozyme Chymotrypsin Ovalbumin Serum albumin Aldolase Urease Ferritin# Ovomucoid# Unknown 1,000,000 14,000 25,000 45,000 68,500 150,000 500,000 700,000 28,000 ⎯ 85 200 190 170 150 125 90 92 160 139 *Blue dextran is not a protein but a high-Mr carbohydrate that has a covalently bound blue dye, and it elutes with the void volume of the column. # Do not…
Given this, if you used 6g of vitamin Z powder to make 20 ml of solution, what is the % concentration of this solution? (I gave the image since I don't know if that info is needed to solve this question.)It also gives a follow-up, if you can help here too: You work in a lab as a summer student. One of your tasks is to make sure that there is enough cell culture medium containing antibiotics to grow bacteria. One day you realize that there is only 5 ml of 10% Antibiotic stock solution in the freezer. You decide to use it all to prepare the working culture medium with 0.01% antibiotic. In the lab there is plenty of growth medium without antibiotics. (Note: dilution in medium is like dilution in water). You remember the equation to make dilutions of stock solutions. You usually use this formula to calculate the required volume of a stock solution, but you realize it can apply here as well, even though the unknown is the final volume. So, you make that dilution. Given that each bacterial…
An Fab fragment binds to lysozyme with a dissociation constant of Ka = 10-11 M. A 1 nM (10-9 M) solution of lysozyme is treated with increasing concentrations of the Fab fragment. At what concentration of added Fab will half of the lysozyme be bound to the Fab? [Fab] 9.9 Incorrect nM

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