You obtained the following raw data when setting up a Bradford standard curve:AbsorbancyBSA (mg/ml)595nm0.22510.31020.4200.51040.6100.72060.8100.91580.9500.980100.990After blanking against a bradford-dH20 sample, the protein concentration of an unknown sample was determined using the same method and anabsorbancy of 0.594 was obtained.Set up a standard curve, excluding outliers (experimental and statistical) and determine the protein concentration in the unknown sample in mg / ml (up to 3significant figures).

The Bradford curve is used for estimating and analyzing the protein which is present in the given…

Answered: You obtained the following raw data…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

Four amino acid samples were subjected to a reverse-phase chromatography set up and yielded the following Rf values. Which among the samples is the most polar? Sample Rf values A 0,49 0.53 0.21 0.55 OD OB
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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…
Given the following data set, which cuvettes could be used to make a standard curve for absorption data, including a zero point? Check all that apply. Cuvette 1: 0.5 ml water Cuvette 2: 0.5 ml 2 mg/dl protein solution Cuvette 3: 0.5 ml 4 mg/dl protein solution Cuvette 4: 0.5 ml 6 mg/dl protein solution Cuvette 5: 0.5 ml 8 mg/dl protein solution Cuvette 6: 0.5 ml Patient 1 sample Cuvette 7: 0.5 ml Patient 2 sample Cuvette 8: 0.5 ml Patient 3 sample Cuvette 9: 0.5 ml Patient 4 sample O Cuvette 1 O Cuvette 9 Cuvette 7 OCuvette 5 O Cuvette 3 OCuvette 8 O Cuvette 2 OCuvette 4 O Cuvette 6.
Draw the Mchelis Menton plot and the Line Weaver Burk Plot using the data given below and find the Vmax and Km from the Plot.
With a stock concentration of 0.2817 g/L, determine each standard's concentrations. What is the mass of iron in the vitamin?
Given a stock protein solution with a concentration of 6 mg/ml, determine the protein concentration of a solution made by mixing 5 μl of the stock with 5 μl of a buffer.
A calibration curve for the absorbance of an unknown is shown below. What would be the concentration of a sample with absorbance of 0.45. Give the answer with the correct unit.
You assay 0.5 ml of 1/2000 diluted egg white for protein, as described in the practical schedule, and the spectrophotometer reading at 595 nm is 0.6. Using the attached calibration curve(click to enlarge), calculate the concentration of protein in undiluted egg white. Give your answer in mg/ml.
A 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.)
You are given a 27 % (w/v) solution of psicose. Molar mass: psicose (C6H12O6) = 180.156 g/mol. ou have a 0.75 mg/mL solution of bovine serum albumin (BSA). You add 1 mL of the 0.75 mg/mL BSA solution into a standard cuvette (1 cm path length), set your spectrophotometer to 280 nm and read the absorbance of this BSA solution. Molecular mass of bovine serum albumin = 66.4 kDa. Molar extinction coefficient (e) of BSA = 43824 M-1 cm-1 (at 280 nm). What absorbance reading will you obtain?
Make a standard curve by using the values given in the table and determine the concentration of unknown sample? Tube 0,5 µg/ µl BSA 0,15 M NaCl Comassi Brillant Blue Solution Absorbance 595 nm 1 0 100 µl 900 µl 0 2 10 µl 90 µl 900 µl 0,105 3 20 µl 80 µl 900 µl 0,233 4 30 µl 70 µl 900 µl 0,41 5 40 µl 60 µl 900 µl 0,455 6 50 µl 50 µl 900 µl 0,589 Unknown Sample 10 µl 90 µl 900 µl 1,2

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