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.
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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.
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- 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?When pure hemoglobin (molecular mass of 64,000 Da) is separated by the following methods, what major molecular mass species do you expect to see? Gel filtration chromotography: Gel filtration with 6M Urea: SDS-PAGE with DDT: SDS-PAGE: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.
- Total protein: Do you think that refractive index could be used as a regular method for serum protein determinations? If yes, what limitations does it have. If not, why not? What are the major interferences in the biuret method? Refractometry method?The protein concentration of a known standard is 100mg/mL If you prepared a serial dilution, mixing 10μL of protein with 40μL of water what would be concentrations of the first 3 dilutions?You want to set up a 1:10 dilution series, so that you can plate a 10-1, 10-2, and a 10-3dilution; however, you only have access to two9 ml dilution blanks. Explain how you could accomplish this task with only two blanks.
- A.How much of 10,000x SYBR safe would you add to 50 ml to make a final concentration of 1x? B.How will you set up the serial dilution? How many tubes do you need? What is the concentration in each? How much LB will you add to each tube? What volume of cells will you add?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).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?
- Using 25 uL of a patient's serum, how much diluent would be needed to create a 1:2 dilution? ______ ulYou 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).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.