1. Lactoferrin is an iron-binding glycoprotein that forms the antibiotic fragment lactoferricin duringdigestion. The protein was isolated from 1.5 liters of ewe skim milk by successive ammonium sulfateprecipitation until a final salt concentration of 70% was obtained. Determine the amount (in g) ofpowdered ammonium sulfate needed in bringing the solution from (a) 0% to 40% saturation and (b)40% to 70% saturation assuming that the volume remains constant.Initial concentration of (NH4)2SO4,% saturation01020304050607080901055Final concentration of (NH4)2SO4, % saturation304050607080Grams of solid (NH4)2SO4 to be added to 1 L of solution176242 314 390 472 561 657117405491 58459421351 43820113571821216125132563188126 19513065260 337270202 281135672101407090761685511 609533365292219146HUGH LATLE1007345738130522815276

Ammonium sulphate is the commonly used salt for protein precipitation and extraction. Under high…

Answered: 1. Lactoferrin is an iron-binding…

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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Gel Running Buffer is made and kept at 14X concentration for storage. We will need 1.5 L of this solution at a concentration of 1X to run our gels. How would we make this solution? I am having trouble understanding the steps to this question, if you could please help me understand it that would be greatly appreciated!
Wh are doing this procedures can you explain? (ex. heating or adding chemicals etc.) 1) Purification of Vitelline from Egg Yolk-Experimental ProcedureMeasure the volume of 3 egg yolks and mix by adding an equal volume of NaCl solution.Extract the mixture with 3-fold volumes of ether and separate the aqueous phase.Do the same procedure 3 times.Mix the sample with water and rinse.It is expected for the protein to collapse.Some more water is added in order to check whether the collapse occurs completely.The sample is centrifuged and the precipitate is dried. 2) Purification of Plasma Albumin and Fibrinogen-Experimental ProcedureAdd ammonium sulfate to 10 ml plasma up to 25% saturation.Separate the collapsed fibrinogen by centrifuge.Increase the saturation level to 33% by adding (NH4) 2SO4.Separate the globulin by centrifugation.Separate prodoglobulins by increasing the saturation level to 46%.Increase the saturation level up to 64% to precipitate albumin.Separate the albumin by centrifuge…
What is the minimum length of the column required to completely separate the amino acids? What is the time required for solvent elution (i.e. time for all amino acids to exit the column)?
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?
A 100 mL of 0.1 M amino acid at pH 1.0, whose pka for the carboxyl group is less than the pKa of the R-group, was titrated with NaOH solution. The pH was monitored, and the results were plotted on a graph, as shown below. The key points in the titration are designated A to G. 12 10 8 pH 6 4 2 0 A B 0.5 с D E F 1.5 2 2.5 Equivalents of OH 1. What is the possible identity of the amino acid? [Select] 2. What is the isoelectric point of the amino acid? [Select] 3. What is the pka corresponding to the deprotonation of the alpha-amino group? [Select] 4. Region/ point where the amino acid is predominantly present as a (-2)-charged species. [Select] 5. The effective buffering range for the amino acid in the basic region. [Select] G 3
1.0 0.9 Z 0.8 15. A pharmaceutical company studied the binding of three different compounds, X, Y, and Z, to a particular protein of interest. For each compound, the fractional saturation (v) was determined as a function of concentration. The results are shown in the figure. Which of the three compounds has the strongest affinity for the protein? Explain. 0.7 X 0.6 > 0.5 0.4 0.3 0.2 0.1 0.0 Y 0.0 0.2 0.4 0.6 0.8 1.0 1.2 1.4 1.6 1.8 2.0 2.2 2.4 2.6 2.8 3.0 L(μM)
Given a stock protein solution with a concentration of 6 mg/ml, determine the protein concentration of a solution made by mixing 5 μl of the stock with 5 μl of a buffer.
1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
The octapeptide gly-cys-met-asn-lys-ala-tyr-gly was hydrolyzed consecutively by CNBr and then trypsin (3 fragments total). The mixture of fragments was buffered at a pH 8.5 and then chromatographed on an anion-exchanger (positive resin) with the same buffer. Draw sequence (abbreviated form) of all fragments at that pH (show charges) and predict elution order.
2.58. Bacteria have equivalent diameters of 2 × 10-6 m and densities of approximately 1 kg/L. Under optimal conditions, bacteria can di- vide every 30 min. Determine the mass of bacteria that would accumulate in 72 hr under continuing optimal growth conditions. Can this occur? Explain.
For paper chromatography, the obtained Rf value of an amino acid with uncharged nonpolar R group is greater than the obtained Rf value of an amino acid with charged polar R goup. TRUE OR FALSE?
calculate the volume of stock solutions required to make up the buffer solutions that will be used for protein purification. The solutions you need to prepare for purification are: i. Binding Solution A: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 5mM imidazole, 5% (v/v) glycerol ii. Wash Solution B: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 75mM imidazole, 5% (v/v) glycerol iii. Elution Solution C: make up 10 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 500 mM imidazole, 5% (v/v) glycerol please show your working . Thnk you

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