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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- Total Protein Determination Spectroscopy Values CREATE CALIBRATION CURVE? DRAWN CONCENTRATION AND ABSORPTION CURVEIn a mixture of five proteins listed, draw an elution profile (Absorbance vs. mL eluted, arbitrary) for the purification of the listed proteins on a gel filtration chromatography resin: cytochrome c (pI = 5.4; Mr = 13,000), immunoglobulin G (pI = 7.3; Mr = 145,000), ribonuclease A (pI = 9.6; Mr = 13,700), RNA polymerase (pI = 6.3; Mr = 450,000), human serum albumin (pI = 5.4; Mr = 68,500). Label your elution peaks. Draw a sketch of an SDS-PAGE, reflecting the mobility of the above mixture as they elute from the column. Label you protein bands.can you show how to calculate the amount of two components for the required volume of a buffer with the receipes? Prepare enough 10X stock solution § Prepare 1LProportions§ 0.25M tris§ 1.92M glycine§ pH 8.3§ 1% (w/v) SDSInstructions to prepare 100mL of 10X running buffer1. Weigh 3.02g of Tris base and 14.42g of glycine into ~90mL of ddH2O in a clean beaker and stir todissolve.2. Check the pH with a calibrated pH metre once dissolved.§ The pH of the buffer should be 8.3. pH adjustment is not required if between 8.1-8.5.3. Add 5mL 20% (w/v) SDS stock solution (a liquid) to make a 1% (w/v) solution.4. Top the volume to 100mL by adding 5mL ddH2O from a graduated cylinder.
- Calculate protein concentration in unknown samples 1, 2, 3: Absorbance of Unknown 1 = 0.541 Absorbance of Unknown 2 = 0.85 Absorbance of Unknown 3 = 1.02 Standard Curve: Y = 0.0073xFrom this standard curve and chart below, does the separation of molecules in the mixture appear successful from the gel filtration? Is there a clearlydefined separation between molecules? Explain your conclusions. Parameters required for calculation of coefficient (Kd) for unknown protein Volume eluted (mL) Which variable does this volume represent in the equation for Kd? Fraction with maximal DNP-Aspartate detected 36 Vt Fraction with maximal Protein detected 24 Ve Fraction with maximal Blue dextran detected 6 Vo2. Provide a one-sentence broad generalization regarding the % acrylamide one should use in SDS PAGE gels and the MW range targeted. 3. Name and give the purpose of each component in the electrophoresis buffer (specify type and pH) used for SDS PAGE.
- 1&3/4 tbs po BID x 7 days #QS How many milliliters should the pharmacy dispense?100ml of LB media with 25 μg/ml of Amp and 100 μg/ml of Kan final concentration. You have 100ml of LB provided and Amp and Kan stocks at 100 mg/ml and 50 mg/ml provided. Determine how much of each antibiotic stock solution you need to add to 100ml of LB to reach desired antibiotic concentration.Solution Absorbance mg/ml aspirin Standard solution - 1.6 mg/mL A 0.638 0.08 mg/mL B 0.504 0.064 mg/mL C 0.376 0.048 mg/mL D 0.259 0.032 mg/mL E 0.126 0.016 mg/mL A = -log T where T = %T ÷ 100 Construct a callibration curve using the above data. Absorbance should be on the vertical axis and "mg/mL of acetylsalicylic acid" on the horizontal axis. The line should go through the origin. Using the data provided, the graph you have generated, and the procedure that was used to generate the solutions which were examined by spectroscopy, calculate the amount of acetylsalicylic acid per tablet. Commercial tablet 1 labelled as 100 mg enteric coated Absorbance = 0.16 Commercial tablet 2 labelled as 300 mg Absorbance = 0.45 Student prepared tablet from practical 5 Absorbance = 0.19 Using the data provided, the graph you have generated, and the procedure that was used…
- If I had a standard with 2.0 mL of Bradford reagent then added 50μL of 250 μL/mL ; what would be the concentration of original protein?I need to prepare a standard calibration curve for gamma globulin. absorbances on Y and mg of standard protein per assay on X. used 0.1mg/ml gamma stock for tubes 2-6. (Water (ml), gamma (ml), Abosrbance)--> (.036, .004, .290) (.036, .008, .358) (.024, .016, .341) (.016, .024, .520) (.008, .032, .597) - What is the math and how do you get the standard curve?An order reads: Daptomycin in NS IV Administer 8 mg/kg over 30 min q24 hrs x 10 days How many milliliters of a vial containing 500 mg of daptomycin in 10 mL should be added to a 100 mL bag of NS to follow the order above to treat a 245-lb patient?