A)- how much volume of the cell of Sykum amino acid analyzer ? B)- Is the Sykum amino acid analyzer column reversed or normal stationary phase ? Or none of them
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- After doing the preliminary studies on redcrest protein extract, Tighnari proceeded with its characterization and analysis proper. He purified the crude protein extract through ammonium sulfate precipitation (40-60%) and gel filtration chromatography. Shown below are the results of the analyses. ||||| 250 kDa Crude Protein Extract 200 kDa 100 kDa 80 kDa 40 kDa 20 kDa ||| || Partially Purified Protein Extract Purified Protein Extract Figure D.1. Electrophoretogram obtained after NATIVE PAGE of the provided protein extracts. PAGE Analysis: 1. Based on Figure D.1., the series of purification procedures led to the isolation of two major redcrest proteins, COL and LEI. Determine the molecular weight of COL and LEI if the results of GFC showed that COL eluted out of the column first.(a) The octapeptide AVGWRVKS was digested with the enzyme trypsin . Which method would be most appropriate for separating the products: ion-exchange or gelfiltration chromatography? Explain. (b) Suppose that the peptide was digested with chymotrypsin . What would be the optimal separation technique? Explain.Explain in details how you could separate a mixture of three amino acids Arg, Lys, and Cys using ion-exchange chromatography. For the toolbar, press ALT F10 (PC) or ALT+FN+F10 (Mac). ...
- In nickel column affinity chromatography,how does the protein binds to column?How is the protein eluted from the column?If 1ml of an unknown sample of protein is diluted to 10ml, and a 0.5ml portion of the diluted sample is found to contain 50ug of protein when assayed for protein using the lowry method. If you mix two unknown samples and repeat the lowry assay, is the absorbance equivalent to the sum of the two individual unknown samples that is used?In a gel filtration chromatography, what type of gel must be used when the protein size is 2500 Da? Explain.
- 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…How can a mass spectrometer be used to identify the protein/s excised from a 2D gel?Given this, if you used 6g of vitamin Z powder to make 20 ml of solution, what is the % concentration of this solution? (I gave the image since I don't know if that info is needed to solve this question.)It also gives a follow-up, if you can help here too: You work in a lab as a summer student. One of your tasks is to make sure that there is enough cell culture medium containing antibiotics to grow bacteria. One day you realize that there is only 5 ml of 10% Antibiotic stock solution in the freezer. You decide to use it all to prepare the working culture medium with 0.01% antibiotic. In the lab there is plenty of growth medium without antibiotics. (Note: dilution in medium is like dilution in water). You remember the equation to make dilutions of stock solutions. You usually use this formula to calculate the required volume of a stock solution, but you realize it can apply here as well, even though the unknown is the final volume. So, you make that dilution. Given that each bacterial…
- What is the isoelectric point of this fragment? DHVTHLRKMGa. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? ExplainYou 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?