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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7. A total of 7.21 g of dry mixture with a protein content of 89.2% (w/w) determined by Kjeldahl analysis was dissolved in 88.54 g of sterile water and centrifuged to purify the protein in the mixture. After centrifugation, a total of 5.95 g of precipitated pellet was formed, and the protein content in pellet was determined as 72.2% by spectrophotometric Lowry analysis. Assume that pellet is not a hygroscopic material and does not absorb any water. Determine the following: a. the protein concentration in the supernatant layer after centrifugation in % w/w b. the nature of amino acids in the protein structure. What's the possible explanation?
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A number of techniques can separate proteins on the basis of their differences in mass. Describe the use of two of these techniques, centrifugation and gel electrophoresis. The blood proteins transferrin (MW 76 kDa) and lysozyme (MW 15 kDa) can be separated by rate zonal centrifugation or SDS-polyacrylamide gel electrophoresis. Which of the two proteins will sediment faster during centrifugation? Which will migrate faster during electrophoresis?
An peptide antibiotic was isolated from one of the nastiest looking bacteria ever viewed. The following observations were made about the peptide. a) Acid hydrolysis yielded equimolar amounts of the following: leu, orn, phe, pro and val. Ornithine (orn) is an amino acid not found in proteins, but is found in peptides. We will see it later when we discuss the Urea Cycle. It has the structure HN-CH,-CH:-CH,--co0 "NH, b) For what it is worth, the molecular weight of the peptide is about 1200. c) When treated with the enzyme carboxypeptidase, an enzyme which degrades peptides from the carboxyterminus, the peptide failed to undergo hydrolysis.( Whoa, we are not in Kansas anymore, Toto!) d) Treatment with fluorodinitrobenzene, which will react with N-terminal amino acids, followed by acid hydrolysis yielded unmodified amino acids and the following derivative of ornithine. Please note where the orn is modified. e) Partial hydrolysis followed by chromatographic separation yielded the following…
b) Consider the following experimental results: Total hydrolysis of a nonapeptide gave: Ala,Arg,Glu,Leu,Lys,Met,Phe,Tyr, Val One fragment from CNBr treatment was: Tyr-Leu-Lys One fragment from Chymotrypsin treatment was Arg-Glu-Met-Tyr One fragment from Trypsin treatment was Val-Ala-Phe-Arg ii. The reagent shown below is widely utilized in the sequencing of peptides. Treatment of the nonapeptide you deduced in part i. with this reagent yields a phenylthiohydantoin derivative, compound 1, and an octapeptide. Write a mechanism for the formation of compound 1. N=c=8
You are analyzing the peptide ala-ile-glu-lys-phe-val- tyr-cys. If you treat the peptide with chymotrypsin, which technique would be best to separate the fragments? O a. ultracentrifugation O b. affinity chromatography O c. dialysis d. gel filtration chromatography O e. ion exchange chromatography What is an advantage of NMR spectroscopy over x-ray crystallography in studying protein structure?
47. Tretinoin gel (RETIN-A MICRO) is avail- able in two strengths: 0.1% w/w and 0.04% w/w. Which of these represents equivalent concentrations of the two strengths? (a) 15 mg/15 g and 30 mg/30 g (b) 5 mg/5 g and 0.06 g/15 g (c) 15 mg/15 g and 60 mg/15 g (d) 30 mg/30 g and 6 mg/15 g 47. (d) 30 mg/30 g and 6 mg/15 g
20. The dissociation constant of protein Z for ligand Y is: 10 micromolar. What fraction of the ligand is bound at ligand concentration = 5 micromolar?
Determine the pI of the peptide H2N-Ala-Lys-Ser-Arg-COOH at pH 11, please explain why some pKas are used in the solution of the problem while others are not.
A rat liver (2 gms) was dissected, homogenized under optimal conditions in appropriate buffer (50 ml), pH, temperature & supplemented with protease inhibitors. The protein level in a 100 μl sample of the homogenate (H) was determined using standard procedures, & was estimated to be 2 mg/ml. Peepo is a medical student interested in purifying a protein that transports copper (Cu) at the expense of ATP hydrolysis into ADP and inorganic phosphate (Pi). Thus, prior to purification Peepo must develop an assay/test that confirms the presence of this protein. Kindly select one answer for Questions 1-10 Question -1 Compared to a control which of the following may serve as a possible assay verifying the presence of a Cu sensitive protein that hydrolyzes ATP: Add Cu to the H and measure the level of Pi Add ATP to H and measure the level of copper Vary copper level, add inorganic phosphate to H & measure residual Pi Vary Cu, add ATP to H and measure level of inorganic Pi…
5 You need to separate the following three proteins, Protein A (MW 76 600 Da; pI 4.5); Protein B (MW 70 000 Da and pI 8.2) and Protein C (MW 42 000; pI 8.6). Describe what column/s you would use, the pH of the buffer/s you would use, which proteins are retained on the column and how you would elute the bound protein/s. How would you monitor where the protein peaks elute and whether the protein in each peak is pure of not?
84. Concentration of a Solution A biologist is trying to find the optimal salt concentration for the growth of a certain species of mollusk. She begins with a brine solution that has 4 g/L of salt and increases the concentration by 10% every day. Let Co denote the initial concentration, and let C, be the concen- tration after n days. (a) Find a recursive definition of C. (b) Find the salt concentration after 8 days.

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