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The absorbance values for different BSA standards. How can the protein concentration be calculated? Which absorbance value should be used?
![Bradford Assay standard curve
1,4
y = 0,0222x + 0,1252 Chart Area
R = 0,9462
1,2
0,6
0,4
0,2
10
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[Protein] ug/ml
Absorbance at 595nm
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- [protein] volume [protein] [protein] in to Sample Lysate in "gel- load 5 in 20 protein in Name volume assay* lysate ready" ul sample protein 3.9 2 µl Hg/ml Tilapia 19.9 10 μι Hg/ml 18.2 2 µl Hg/ml Cod >20 14 10 μι Hg/ml 9.4 15 2 µl ug/ml Sole >20 6. 10 μι ug/ml > >Electrophoresis A protein required 6.8 min to travel 82 cm to the detector in a 96 cm -long capillary tube with 25.4 kV between the ends. Find the apparent electrophoretic mobility.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?
- Q4 (a) SDS-PAGE. Sodium dodecyl sulfate - polyacrylamide gel electrophoresis (SDS-PAGE) is used to identify the molecular weight of unknown protein samples. Briefly outline the principle of SDS-PAGE. Marks: 2 For the toolbar, press ALT+F10 (PC) or ALT+FN+F10 (Mac). BIUS E v E Y A ... Paragraph Arial 14pxIn SDS PAGE the resolving gel : is 4%(w/v) acrylamide,PH )6.8 is 6-20% (w/v) acrylamide is 4%(w/v) acrylamideA series of bovine serum albumin (BSA) was prepared and 1 mL of each solution was subjected to a Bradford assay. The increase in absorbance at 595 nm relative to the concentration of protein was plotted as shown below. Save 1.0- 0.8- 0.6- 0.4- 0.2- 0.04 0.0 0.5 1.0 2.0 2.5 1.5 BSA concentration (mg/mL) a) Using the graph, calculate the original concentration of protein present in a mixture of haemoglobin and methylene blue (diluted 1:50), which gave an absorbance of 0.20 at a wavelength of 595 nm using the Bradford assay. Show all workings. Absorbance (O.D.)
- For the following sequence, what is the approximate annealing temperature? 5'-AGCTACGATCAGGTCA-3'A 1/10 dilution of enzyme extract has been done for the protein assay. The experimental results are given below. Tube Phosphate buffer 0.1 M pH 7 (µL) Diluted enzyme extract (uL) Bradford reagent (mL) DO at 595 nm 0,8 0,7 0,6 0,5 0,4 0,3 0,2 0,1 A595 0- 0 1 50 50 1 0.102 1- Calculate the mass of proteins contained in 50 or 100 μL of diluted extract thanks to the calibration curve (graph below), performed with serum albumin (SAB). 2- Calculate the protein concentration of undiluted enzyme extract. 2 3 5 50 50 0 50 50 100 100 1 1 1 1 0.098 0.101 0.199 0.200 2 6 8 10 SAB (ug per tube) Data: the slope of the calibration curve is 0,05 µg¹¹. 4 0 12 14 6 0 100 1 0.200 16(b) Both laboratories used 10 micrograms of protein each in their kinetic assays. Protein concentrations weredetermined by the Bradford protein assay. Assay conditions employed in the two labs (pH, temperature,etc.) were also identical. What would be the most plausible cause for the discrepancy in the Vmax valuesfor the compound I? Explain.Recall that the Bradford assay measures total protein amounts in sample solution based on complexformation between a dye and proteins. Also, the assay solution used in both labs does not contain anyinhibitors.
- In 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.The A280 of a protein sample loaded onto a gel was determined to be 0.767 (1.00 cm path length, after subtracting the blank). The total volume of this sample was 428 µL. 19.0 µL of this protein sample was mixed with 19.0 µL of 2X laemalli sample buffer and then 12.0 µL of the entire sample was loaded into the gel and electrophoresed. Calculate the amount of protein that was loaded into the gel (in µg).Sketch the appearance after visualization of a protein mixture containing the seven proteins (fibrinogen, y-globulin, collagen, ovalbumin, myoglobin, hemoglobin, insulin) when subjected to two-dimensional (2D) gel electrophoresis.