Özcan MM. and his colleagues tried to obtain 3different fatty acids from moringa pelegrinanucleus with cold pressing and soxhletextraction by two different methods. The data isas follows;Fatty acidsCold pressing methodMoringa pelegrina nucleusSoxhlet extraction methodMoringa pelegrina nucleusa-tocopherol(mg/kg) 137.89 ± 2.89y-tocopherol(mg/kg) 63.68+0.878-tocopherol(mg/kg)151.67+1.8971.57+1.0661.49+0.7663.58+0,97Accordingly, 3 different fatty acids obtained by 2different methods used;a) Calculate their efficiency.b) By which method has more efficiency beenachieved and explain with the reasons?

Efficiency refers to the amount of the product produced from the source. Here it will expressed in…

Answered: Özcan MM. and his colleagues tried to…

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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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…
(a) 1 Normalized fluorescence 0.8 0.6 0.4 0.2 0 50 55 OM 0.100 M 0.200 M 0.300 M 0.500 M 1.00 M 2.00 M 60 113588 65 Temp. (°C) 70 75 80 Where is fully folded protein? • Where is fully unfolded protein? • Where is partially folded protein? • To what does SYPRO orange bind? • Why does fluorescence increase as a function of temperature? ● Define a melting temperature for a protein. • Demonstrate how an estimated melting temperature of the protein in zero molar ligand can be determined. • What is the effect of increasing the molar concentration on melting temperature for this protein? • Why is melting temperature a useful measurement to make for a protein especially if you are interested in protein aggregation?
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)?
G418 disulfate (FW 692.7) is an antibiotic used to select transfected mammalian cells in tissue culture. The standard working concentration for selection is 400 µg/mL of active ingredient in culture medium. The bottle states that it contains 71% active ingredient. You need to make a 100x stock in medium and adjust the pH before you apply it to cells. How much powder should be added to make 10 mL of stock solution? How much do you add to a 2 mL culture dish?
80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pI. The solution is then titrated with 0.2M HCL to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCL needed to reach relevant pKa value and equivalence point(s)z Relevant pKa values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
You are trying to separate study Fibrinogen variants with a pl approximately 5.8. Which ion exchange resin would you use under the different conditions proposed? O Carboxymethyl at pH=2.8 O Alkylsulfonyl at pH=7.0 O DEAE at pH = 7.0 O Quaternary alkylammonium resin at pH=2.8 O DEAE and Carboxymethyl approaches could both work.
This is a visible spectra between 390-590 nm obtained during the protein separation process of haemoglobin and cytochrome c using CM Sephadex chromatography. I'd like the results shown on the image interpreted. Look for characteristic peaks or patterns that correspond to the absorption properties of these proteins in the visible range.
Hand draw the expected gel result from the graphical data of three extracted RNA samples (in Figure 1a, 1b, & 1c) in Nanodrop spectrophotometer. The 3 graphical data should be in 1 agarose gel Provide complete gel label descriptions (ladder, lanes, etc.).
Does this calculation look correct? My goal isto have a target mass of 10 µg of my protein with a total volume of 30 µl. Protein was measured and found to have a concentration of at 308.35 µg/ml Recall, mass = concentration * volume 10 µg = 308.35 µg/ml * V V = 0.01 mg/ 0.30835 mg/mL = 0.032430679 mL = 32.43067942 µL Note: cannot measure this amount; two dilutions required. Dilute by 1/40: measure 2.5 µl of protein at 0.30835 µg/µl and add it to 97.5 diluent to prepare a solution of protein at 7.71 mg/ml. This diluted sample will be used further. Mass = concentration * volume 10 µg = 7.71 mg/ml * V V = 0.01 mg/ 7.71 mg/ml = 1.3 µL Therefore, will measure 1.3 µl of protein at 7.71 mg/ml and add it to 28.7 µl of diluent.
Can Hydrophobic Interaction Bead Chromatography be used to isolate Protein X from muscle tissue if Protein X contains many hydrophobic regions? Explain the process of how to isolate Protein X from muscle tissue.
A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).
What is the chemistry behind of the effect of proteins when it is subjected to different temperatures done in three trials? see the data below to interpret Table 3.1 %Transmittance of Identical 10% albumin samples subjected to different temperatures done in three trials. Heating Tempt. (C) %Transmittance Trial 1 Trial 2 trial 3 Average Control (unheated) 62 62 62 62 55 60 59 58 59 60 2.5 4.5 4.5 11.5 65 1.52 1.6 1.52 1.55 70 1 1 1 1 Table 3.2 Absorbance of Identical 10% albumin solution subjected to different temperatures done in three trials. Heating Tempt. (C) Absorbance Readings (450nm) Trial 1 Trial 2 Trial 3 Average Control (unheated) 0.2076 0.2076 0.2076 0.2076 55 0.2218 0.2219 0.2366 0.2292 60 1.6021 1.3468 1.3468 0.9393 65 1.8182 1.7959 1.8182 1.897 70 2 2 2 2

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