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- Can you answere this question pleaseYou run 5 standard proteins listed below on a size-exclusion (gel filtration) column with limit of 200,000Da. Please draw a chromatogram on a separate page with each peak and both axes labeled. Protein B-Amylase Alcohol dehydrogenase Bovine albumin Carbonic anhydrase Cytochome A280 MW 223,800 0.5 82,000 0.6 66,463 0.45 30,000 0.43 12,000 0.8Example of a Protein Purification Scheme: Purification of the Enzyme Xanthine Dehydrogenase from a Fungus Volume Total Total Specific Percent Fraction (mL) Protein (mg) Activity Activity Recovery 1. Crude extract 2. Salt precipitate 3. Ion-exchange chromatography |4. Molecular-sieve chromatography 5. Immunoaffinity chromatography 3,800 22,800 2,460 0.108 100 165 2,800 1,190 0.425 48 65 100 720 7.2 29 40 14.5 23 1.8 275 152.108 11 Calculate the specific activity of step#4. Note that percent recovery=% Yield.
- Also please explain why you chose the column based on the column and the protein propertiesConsider the proteins in the table below. Protein Isoelectric point (pl) М.W. Alcohol dehydrogenase 150,000 5.5 Cytochrome C 12,400 10.5 Serum albumin 66,000 5.3 B-Amylase 200,000 5.7 Apoferitin 443,000 4.0 Fill in the blank. If the mixture of proteins above was subjected to anion exchange chromatography at pH 8, from the column. would be the first protein to eluteA Biochemist perform different experiments involving ELISA in order to determine the amount of cofactor that can be captured by a protein. The biochemist plot log of the absorbance v.s log of the concentration. The concentration was prepared in a nM. The equation of the line is Y=0.9988 x -1.437. Calculate the absorbance that produced if the concentration is 1.25 nM.
- 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).Given the data, discuss the following results of a hypothetical Biochemical test performed on 4 bacterial isolates .What would be the best buffering agent to choose if you wanted to buffer an enzyme reaction or tissue culture medium at pH = 7.95? Group of answer choices a. HEPES (4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid); pK = 7.5 b. Histidine; pK1= 1.78; pK2= 5.97; pK3= 8.97 c. Bicarbonate; pK = 6.1 d. Phosphate; pK1 =2.0, pK2 = 6.8; pK3 = 12.5 e. Tris or Tris(hydroxymethyl)aminomethane; pK = 8.07
- 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.nfile.php/7382360/mod_resource/content/0/Pyrimidine%20Practice%20Pat 1 / 1 67% + | 田 Pyrimidine Synthesis El * be surc to label reguletary Steps K carbamay1 phiuphate E2 orotate R-5P Eg UMP d TMP ATP ADPEE3 TET EedUDP O dumP E4 E5 CTP-> dCDPChoose the correct description for the Biomolecule Test demonstrated in the figure. reagent త The polysaccharide starch is tested using Lugol's lodine The protein is tested using Biuret Reagent. The protein is tested using Lugol's lodine The polysaccharide starch is tested using Biuret Reagent O O O