This graph represents a standard curve from a BCA assay for protein concentration. If your BCA reaction with your unknown protein has an absorbance of 0.2, approximately what concentration of protein is in your unknown sample? Absorbance (562nm) 0.5 0.45 3 0.35 0.3. 0.25 0.15. 0.1- 0.05 [Protein (BSA)) (pg/ml) 10

This graph represents a standard curve from a BCA assay for protein concentration. If your BCA reaction with your unknown protein has an absorbance of 0.2, approximately what concentration of protein is in your unknown sample? Absorbance (562nm) 0.5 0.45 3 0.35 0.3. 0.25 0.15. 0.1- 0.05 [Protein (BSA)) (pg/ml) 10

Curren'S Math For Meds: Dosages & Sol

11th Edition

ISBN:9781305143531

Author:CURREN

Publisher:CURREN

Chapter13: Dimensional Analysis/units Conversion

Section: Chapter Questions

Problem 1.8P

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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?
You perform a Bradford assay to determine the concentration of isolated α-lactalbumin. You use 50 μL of a two-fold diluted solution of α-lactalbumin in the assay. You generate a standard curve with the following equation for the line: y = 0.163x + 0.082. The absorbance of your sample was 0.674 AU. What is the concentration of α-lactalbumin, in mg/mL, in your sample? Give your answer to three significant figures.
Using Bradford Assay, plot the standard curve and find the unknowns. Protein Concentration A595 of sample 0 0 3 0.220 6.5 0.383 12 0.667 18.8 0.930 24.2 1.090 Unknown 1 1.085 Unknown 2 0.708 Unknown 3 0.193
You obtained the following raw data when setting up a Bradford standard curve: BSA (mg/ml) Absorbancy 595nm 0 0.225 1 0.310 2 0.420 3 0.510 4 0.610 5 0.720 6 0.810 7 0.915 8 0.950 9 0.980 10 0.990 After blanking against a bradford-dH2O sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.570 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 3 significant figures).
1.0 ml of serum albumin (BSA) solution was precisely diluted to 100 ml with a buffer solution, and the absorbance at 280 nm was measured from this buffer solution at a distance of 1 cm from the light. The result was A=1.0. BSA is 0.1%(=0.1g/l). The absorptivity is e(0.1%)=0.667, so 1g/l solution gives an absorbance of 0.667. What was the original protein content? Report in the result unit mg/ml with an accuracy of 0.1 mg.
In the experiment performed for the determination of cholesterol, the function of the calibration curve obtained using 25-400mg/dL standard cholesterol solutions was determined as y= 0.0009x. If the absorbance of the serum sample is determined as 0.28, what is the amount of cholesterol in the sample, in mg/L?
You obtained the following raw data when setting up a Biuret standard curve: BSA (mg/ml) Absorbancy 540nm 0 0.158 1 0.210 2 0.260 3 0.305 4 0.360 5 0.410 6 0.455 7 0.510 8 0.530 9 0.550 10 0.554 After blanking against a biuret-dH2O sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.284 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 3 significant figures).
Using the equation for the best-fit straight line through your data, the average absorbance of your unknown samples U1 and U2, and any dilution factors (DON’T LEAVE OUT THE DILUTION FACTOR), calculate the concentration of protein in the original unknown protein sample. y = 1.6849x + 0.0414R² = 0.9904
4 mL of 10% TCA solution was added to 1 mL of serum and after mixing, it was waited for two minutes and filtered through non-phosphorus filter paper. 1 mL of the filtrate was taken and 13 mL of distilled water, 4 mL of sulfomolybdic acid and 2 mL of dilute SnCl2 solution were added and mixed, and after waiting for 15 minutes, the absorbances of the obtained solutions against pure water at 520 nm were read. If the function of the calibration graph obtained with 0.5-2.5 mg/mL standard phosphorus solutions is y= 0.245x + 0.107 and the absorbance value of the serum sample is 0.109, what is the amount of phosphorus in the sample?
In the experiment performed for the determination of cholesterol, the function of the calibration curve obtained using 25-400mg/dL standard cholesterol solutions was determined as y= 0.0009x. If the amount of cholesterol in the serum sample is determined as 3.11 g/L, what is the absorbance value of the sample? A. 0,280 B. 0.028 C. 0.208 D. 0.82
From 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 Vo
What is the approximate rate of change of A340 measured? i.e. ΔA340 / min = __________ What rate of change of A340 would you predict if 30 ml of the ADH solution was tested in the same way (i.e. half the amount of protein) ? i.e. ΔA340 / min = __________ What rate of change of A340 would you predict if 60 ml of a 0.5 μM ADH solution was tested in the same way? i.e. ΔA340 / min = __________ As well as writing your answers, explain your reasoning.