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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Similar questions

What are the components of the buffers used for protein hydrophobic column chromatography and explain how do they work?
Please describe the protein purification process with the aim of purifying a protein which locates on nucleus membrane.
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
What is the biochemical basis for the spectrum of fastidiousness seen in the microbial world? (That is, why are some organisms fastidious and others are non fastidious?)
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?
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?
A bacterial culture is grown using either octadecane (C18H38) or pentachlorophenol (C6HOCl5)) as the sole source of carbon and energy. The cell yield value is determined by dry weight analysis to be 1.49 for octadecane and 0.05 for pentachlorophenol. Using either octadecane or pentachlorophenol, please describe the steps taken (and the final result) showing what percentage of the substrate carbon will be found as cell mass and as CO2? Please show all calculations and give correct answers.
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…
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?
On the right the Hill plot com- (b) pares the O2 binding properties of Hb Ya- kima with those of HbA in 0.1 M NaCl buff- Hb-Yakima ered to pH 7 with 0.01 M bis-Tris. Focus first on the line for "stripped Hb". This is the term for hemoglobin isolated from erythro- cytes with removal of all organic phosphate molecules that might bind to the protein in RBCS. You can see that 2,3-bisphospho- glycerate (BPG; labeled DPG according to old terminology) does not alter the O2 bind- ing affinity of Hb Yakima in contrast to HbA (although it was shown that BPG did bind to the deoxyHb Yakima molecule). Also, Hb Yakima is associated with markedly decreased allostery in the absence and presence of BPG, in comparison to HbA. IHP = inositol hexaphosphate, an artificial allosteric modifying ligand that binds more tightly than BPG. stripped Hb Hb-A •DPG +DPG n= 1.0 n = 2.3 n=2,5 +THP +IHP 0.5 0.5 1 5 10 50 po, ( mm Hg ) %3D On the right is a diagram copied from the lecture handout "Hemoglobin and Allo-…
Explain the Rf value obtained on the basis of the structure of amino acids use. Explain in 1-3 sentence only.
13. 0.9% (m/v) NaCI solution and 5% (m/v) glucose solution are both isotonic to red blood cells. SHOW your work and watch sig figs & units. c. convert the concentration from M to % (m/v) for a 0.342 M NaC solution. (HINT: convert to g/ml and then multiple by 100%)

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