Q9) Given the following sample preparation 200 microliters of BSA (protein) at 240 micrograms/ mL 50 microliters H2O 1000 microliters of Lowry Reagent 100 microliters of Folin Reagent How would you prepare a blank tube? What is the purpose of the blank?
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Q9)
Given the following sample preparation
200 microliters of BSA (protein) at 240 micrograms/ mL
50 microliters H2O
1000 microliters of Lowry Reagent
100 microliters of Folin Reagent
How would you prepare a blank tube?
What is the purpose of the blank?
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- 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…a. State the importance of using following reagents in SDS-PAGE. 1. Acrylamide 2. Bisacrylamide 3. Tetramethylethylelediamine 4. Glycerol 5. Ammonium persulfate b. Briefly describe the importance of two dimensional electrophoresis in protein separation?AE, 62, Male Wt: 75 kg, Ht: 150 cm Orders: Penicillin G Potassium 10,000,000 Units Sterile water for injection qs Make a 250,000 U/mL solution. The package insert states If Penicillin G Potassium 10,000,000 Units is reconstituted with 44 mL sterile water, a solution of 200,000 U per mL will be obtained. What volume of sterile water would you use to reconstitute the penicillin G potassium in order to make the ordered solution?
- Total Protein Determination Spectroscopy Values CREATE CALIBRATION CURVE? DRAWN CONCENTRATION AND ABSORPTION CURVEThe correct order of steps when purifying a protein are: Group of answer choices 1)Growing bacterial culture for fusion protein; 2)Harvesting IPTG-induced cultures; 3)Lysing bacterial cell; 4)Removing insoluble debris; 5)Using Affinity Chromatography to purify protein. 1)Growing bacterial culture for fusion protein; 2) Breaking open bacterial cells; 3) Removing insoluble debris: 4) Harvesting IPTG-induced cultures; 5)Using Affinity Chromatography to purify protein 1) Growing bacterial culture for fusion protein; 2) Lysing bacterial cells; 3) Harvesting IPTG-induced cultures; 4) Removing insoluble debris: 5)Purifying protein by affinity chromatography 1)Growing bacterial culture for fusion protein; 2) Removing insoluble debris; 3) Harvesting IPTG-induced cultures; 4)Breaking open bacterial cells; 5)Purifying protein by affinity chromatographyThe calibration curve shown below was used to analyze an unknown protein solution. What is the concentration of the unknown solution, if the absorbance of the unknown is 0.505? Answer in ug/mL. 1.2 y%3D0.005x+0.061 R=0.992 0.8 0.6 0.4 0.2 50 100 150 200 250 Concentration ug/ml Absorbance
- Calculate the appropriate volume (in µL) of 3X loading buffer that should be added to 24.0 µL of a sample prior to loading the sample on an agarose gel.C. Choosing the Proper Buffer Solution 1. Choosing the Proper Buffer Solution In Protein Precipitation, two liters of 5mM buffer solution with pH 5.2 is needed in the isolation of albumin. Which among the following buffer solution is best fitted for said purpose? Justify your answer. Buffer solutions pKa Acetate buffer 4.73 Tris- (hydroxymethy) aminomethane 8.08 Phosphate buffer 7.20 Discussion: 2. Preparation of the Chosen Buffer System Calculate and measure the amounts (in grams if solid and in mL if liquid) of weak acid and conjugate base needed to be able to prepare the chosen buffer system in part A above. Express your answer in useful units (that is, prepare it from practical amounts or concentrations of starting materials). D. Titration of an Amino acid Graph: titration of Glutamic acid Glu Glu Glu" Glu- COOH Co0 co0 Co0 H,N*-C -H H,N-C-H H,N*-c-H H,N -C -H CH2 CH2 CH, CH2 CH CH, CH, CH2 COOH соон co0 Co0 14 12 10 pK pH pkg Isoelectric point pk, 1.0 2.0 3.0 Equivalents of COH"…Streptomycin sulfate 400 mg IM daily is ordered for a child weighing 77lbs. The recommended dosage is 20-40 mg/kg/day once daily. A 1 gram vial of streptomycin sulfate is available in powdered form with the following instructions: Dilution with 1.8 mL of sterile water will yield 400mg per mL. If safe, how many mLs will you give?
- Apple puree was analyzed for petulin by HPLC-MS-MS after SPE clean-up. The procedure was 10.0g of puree + 10μl of a 10μg/ml solution of isotopically labeled petulin as internal standard were treated with 10.0ml of pectinase and acetic acid, centrifuged, and filtered. Four ml of the filtrate was passed through a SPE cartridge. The petulin was eluted with 2.0ml of ethyl acetate. The sample was evaporated to dryness and the residue dissolved in 1.0ml of the mobile phase. The analyte signal was 127 and the internal standard 197. Calculate the concentration of petulin in the sample in μg/g (RRF=1).Consider a crude extract with a mixture of the 5 proteins listed below. Protein A 4.5 pl 160 molecular weight, kDa Protein B 12.5 pl and 65 molecular weight Protein C 5.0 pl, 15 molecular weight Protein D 6.8 pl, 150 molecular weight Protein E 9.5 pl, 45 molecular weight You load this protein mixture onto an anion exchange column at pH 11. Next, you apply a "washing" step by passing through buffer at pH 11. Finally, for your elution step, you apply a pH gradient starting from pH 11 to pH 2.0 (A gradient buffer system allows you to gradually and continuously change the pH of your mobile phase starting from pH 11 up to pH 2). You load this same protein mixture onto a Size Exclusion column. Please indicate the order in which these proteins will elute for both. Group of answer choices Yes or No, please explain your answer. If your protein of interest is protein A, would using anion exchange column be completely successful at separating it from all the other proteins? Group of answer…1) You have been asked to make up four 1.5% agarose gels at 30 ml each. Ethidium Bromide is to be added at 0.5 ug/ml and you have a bottle at 10ug/ml. Write down step-by-step protocol of how to proceed. 2. How would you make up one liter of 1X TAE buffer using a 25X stock?