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. O Save 1.0- 0.8- 0.6- 0.4- 0.2- 0.04 0.0 0.5 1.0 1.5 2.0 2.5 BSA concentration (mg/mL) a) Using the graph, calculate the original concentration of protein present in a mixture haemoglobin and methylene blue (diluted 1:50), which gave an absorbance of 0.20 at Absorbance (O.D.)
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- You will be given 1 mL of a 2.0 mg/mL solution of bovine serum albumin (BSA) and 1 mL of a 2.0 mg/mL solution of bovine gamma globulin (BGG). From these solutions, you will need to make 100 μL of each of the following standards using 1x MBP purification buffer as the diluent for preparation of a standard curve: 1000 μg/mL, 750 μg/mL, 500 μg/mL, 250 μg/mL, 125 μg/mL, and 0 μg/mL.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 ~0.1 μg/ml ~4.5 μg/ul less that 0.005 | 0.2 μg/μ. [Protein (BSA)) (pg/ml)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?
- 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.A gel filtration column was calibrated by measuring elution volumes for two proteins of known mass: glutamate dehydrogenase, 290 kDa with elution volume 20.8 mL; serum albumin, 37 kDa with elution volume 42.5 mL Use these values to determine the equation of the straight line graph that relates log molar mass to elution volume. The elution volume of an unknown protein was 32.2 mL. Use the equation just determined above to estimate the molar mass of the protein in kDa units. Don't round your answer until the end to ensure your answer is within the accepted range. Round your answer to the nearest whole number (e.g. If you calculated 27.52, input your answer as 28).How is 10^4 derived? Please show all calculation steps. # of cells per mL = (Average)*DF*10^4
- After blood collection, the red cells are separated from the serum to be used for the preparation of the stock solution. How is it done? For the serial dilution, your stock solution must have a concentration of 3.5 mg/mL. How much diluent must be added to the 5.3 mg/mL red cell to prepare the stock solution? Show pertinent solution/s. What is the appropriate diluent used for the preparation of the red cell suspension?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?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?
- The accompanying figure is from an electrophoresis experiment using SDS–PAGE. The left lane has the following standards: bovine serum albumin (MW 66,000), ovalbumin (MW45,000), glyceraldehyde 3-phosphate dehydrogenase (MW 36,000),carbonic anhydrase (MW 24,000), and trypsinogen (MW 20,000).The right lane is an unknown. Calculate the MW of the unknown.The 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 AbsorbanceYou have an order for 1 gram of Cefazolin in D5W 100 ml. You have added 5 ml of sterile water to the 1 gram vial to reconstitute powder. However the recommended manufacturer’s diluent amount is 10 ml of sterile water for a final concentration of 100 mg/ml. How would reconstituting the vial with 5 mls affect the concentration and the final calculated dose. Please answer with explanation ASAP. I will really upvote. Thanks