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- Name one purification method that can separate Protein A from a solution that contains all four proteins. (Size exclusion chromatography, ion exchange chromatography, Purification by affinity chromatography, High pressure liquid chromatography, Isoelectric focusing, SDS-PAGE, or Two-dimensional Electrophoresis) 2. In picture 3. In picture 4. In picture 5. In picture1. List down the amino acids in the following format Amino Acid Physiological Significance 3 letter Code 1 letter code Chemical Structure 2. List down the different qualitative and quantitative tests for Amino Acids Test Reagents Principle Positive Reaction/ResultA C2 G This a photograph of an actual polyacrylamide gel that has been run with samples of protein. For each question, write the letter from the item in the gel that best matches the word or concept that is described. Answers may be used once, more than once, or not at all. There may be more than one correct answer per question. 1. Band 2. Lane 3. Well 4. Will protein migrate through the gel from A to B or will it migrate from B to A? 5. Which end is nearest the negative electrode, A or B? 6. Which contains smaller protein fragments, F or G? 7. Which letter indicates the highest concentration of protein fragments that are the same size 8. Where would a sample of protein be loaded? B.
- What's the amount of protein if the measurement at A280 = 1.120, dilution factor is 100 and total volume of extract is 45Wh 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…SDS-PAGE gels are useful in determining the molecular weights of proteins; however, the molecular weights of are usually not reliable. protei
- 1. suggest a simple procedure (or test) to veify if the final prodeuct you obtained from the extraction of casein in milk is indded casein. 2. what are the three general steps involved in isolation of proteins> discuss briefly and describe the purpose of each step. 3. what is the purpose of ethanol in the isolation of casein from milk.a protein pretreated with an sds page detergent shows two bands around 100 and 150 kD on the electrophoresis gel.Same protein is treated with the SDS and 2-mercaptoethanol reveal a single band 50 kd on gel.How many subunits would this protein contain3 i. Define Biological Value (BV) of Proteinsii. What are the advantages of this protein evaluation method when compared to Nbalance and chemical score?5iii. A bull consumes 7 kg DM of feed containing 60 g N/kg. The bull excretes 120 g N inthe faeces and 50 g N in the urine. The feacal and urinary N had 20 g metabolic feacalnitrogen (MFN) and 6 g endogenous urinary nitrogen (EUN) respectively.Calculate the BV of the protein in the diet.
- 2. Vasopressin, a substance produced by the human body that regulates blood volume and pressure, is a nonapeptide with the following amino acid sequence. Describe the results you would expect when vasopressin is tested with the following reagents. sort GLY-ARG-PRO-CYS-ASN-GLN-PHE-TYR-CYS test xanthoproteic Millon's Hopkins-Cole nitroprusside observation A 250 25d ZYN CZ, ZINTEG DST ZWIf the absorbance at540nm of a biuret and protein solution containing 0.25mg/ml of protein .24 the absorbance of a biuret and protein and dna solution containing.25mg/ml of protein and 0.5mg/ml dna should be note the total volume is the same in both solutions 0.24 0.72 0.48 not enough inforAll nucleic acid samples regardless of conformation and type will use the same absorption constant of 50 ng/ul for A260-1. O True False