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- The soxhlet extraction method was applied to a solid food sample that matrix effects are expected to be significant for the total lipid analysis. The sample was directly subjective for extraction, and ethanol was used as the extraction solvent. (a.) Outline the typical procedure of the Soxhlet extraction method (b.) Calculate the per cent lipid of the food sample if the result is as following: -Food sample: 12.5755 g -Initial weight of the solvent flask: 30.5697 g -Weight of the solvent flask treated with the ethanol: 30.6271 g -Weight of the solvent flask treated with the sample: 34.0293 g (c.) The value of total lipid content obtained from (b) was much lower than that expected. Suggest three possible reasons and the respective modification improve the analysis.Imagine you are attempting to separate these three dipeptides from each other using anion exchange chromatography, and you use a protein assay to identify at what salt concentration each of them is eluted from the column. A graph showing protein concentration as a function of salt concentration is shown below the dipeptides. Which of the three dipeptides is represented by peak #3? (NOTE: the dipeptides are shown in their non-ionized forms. You must assume that they are in aqueous solution at physiological pH, ~7.2) a) Dipeptide A b) Dipeptide B c) Dipeptide CFor the determination of Pb in blood, a 5.00 mL sample was treated with trichloroacetic acid to precipitate the proteins. After centrifugation, the resulting solution was brought to pH 3 and extracted with two 5 mL portions of methyl isobutyl ketone containing the lead complexing agent APCD (ammonium 1-pyrrolidine carbodithiolate). The extract was drawn directly into an air-acetylene flame which produced an absorbance of 0.444 at 283.3 nm. Two 5.00 mL aliquots of solutions containing 0.250 and 0.450 ppm of Pb were subjected to the same sample treatment and the absorbance that occurred was 0.396 and 0.599 respectively. Calculate the concentration of Pb in µg/dL in the blood.
- 1. A mixture of proteins (pepsinogen, myoglobin, and cytochrome c) is subjected to anion exchange chromatography at pH 5.0. In what order would the following proteins be eluted from the DEAE cellulose anion exchanger by an increasing salt gradient: cytochrome c (pl, 10.6), pepsinogen (pl, 1.0) and myoglobin (pl, 6.8)A protein consists of two types of peptide chains (A and B) with an unknown stoichiometry (AxBy). When you ran this protein directly on reversed phase-HPLC with UV monitor set at 280 nm, two peaks were resolved. Mass spec determined that the peaks represented Chain A and Chain B, respectively. The peak area is 500,000 for Peak A (Chain A) and 100,000 for Peak B (Chain B). The molecular masses of Chain A and Chain B are 25,000 and 5000, respectively. The extinction coefficients for Chain A and Chain B are 1 mL/mg.cm and 0.5 mL/mg.cm, respectively. Please calculate x/y.Protein ABC is a heme-containing protein responsible in electron transfer in microalgae. The target protein was extracted using ammonium sulfate fractional precipitation and quantified using Bradford assay. A set of solutions with increasing concentration was prepared using 15.00 mg/mL analogous protein standard [refer to succeeding table]. Each solution was treated with 80 μL of Bradford reagent and diluted to 1.500mL. The absorbance at 595 nm of each solution was obtained and presented below. Volume of protein std, μL A595 0 0.0002 10 0.0007 25 0.0075 50 0.0165 100 0.0356 250 0.0930 500 0.1950 750 0.3010 1000 0.4175 Report the equation of the calibration curve and proof of linearity (R2 value).
- Biuret Assay accurately quantify protein concentration within the range of 5-150 mg/mL. JUSTIFY THE STATEMENT.In order to improve the peptide separation by using a HPLC system, trifluoroacetic acid acts as mobile-phase modifier was added during the preparation of mobile phase. The preparation was performed by a postgraduate student as following:“2.851 g trifluoroacetic acid (MW: 114.02 g/mol) was made up to 500 cm3 in a graduated flask. To this solution, 50 cm3 of ethanol was added, and after mixing the mobile phase was placed in the solvent reservoir and pumping was commenced at 1.5 cm3 min-1.”Based on the given preparation procedure, identify THREE mistakes that were made.Below are responses generated using the isolated guinea-pig ileum preparation to determine a pA2 value for the cholinergic antagonist homatropine.Responses are expressed in millimetres +/- SDM (n = 4).Plot the data and then determine by Schild analysis the pA2 value and Schild slope. show calculationsWhat conclusions can you draw; does the experiment/data fulfil the criteria for a valid Schild analysis?
- Proteins A, B, and C have isoelctric points of 8.2, 6.7, and 5.2 respectively. Place proteins A, B, and C in order of increasing volume on a size exclusion column. Then place the proteins in order of probable increasing elution volume in cation exchange chromatography during an increasing salt graditend run at pH 5.. An Analytical Chemist is analyzing a protein sample analysis using a light scattering technique. If the formulation of the subject sample has included surfactants or salt additives, which of the following would adequately apply? . The additives would impact the ionic strength of the sample B. The impact of additives influence can be nullified when using a Light Scattering technique. C. The effect of formulation additives would impact the protein sample analysis, and should be considered as a factor when analyzing the protein aggregation using light scattering technique.what is Optical rotatory dispersion and circulatory dichroism method for protein binding?