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.
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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.
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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.After performing the manual Albumin assay, you get the absorbance value of 0.205 for a 4.5 g/dL albumin standard and 0.114 for control A. What is the calculated value of the control? (just write a number with one decimal, the units will be mg/dL)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)
- 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.)A vial of Doxorubicin reads 0•5g per vial. Instructions say to reconstitute each 12mg with 2•5ml of NS. How many ml of NS will be needed to reconstitute the vial of the recommended concentration? please show workingHow is 10^4 derived? Please show all calculation steps. # of cells per mL = (Average)*DF*10^4
- If 1ml of an unknown sample of protein is diluted to 10ml, and a 0.5ml portion of the diluted sample is found to contain 50ug of protein when assayed for protein using the lowry method. If you mix two unknown samples and repeat the lowry assay, is the absorbance equivalent to the sum of the two individual unknown samples that is used?Enzyme X has a molecular weight of 48,000. It converts substrate Z into product Y. Z absorbs at 340 nm, and Y absorbs at 480 nm. A.) At what wavelength would you measure the change in absorbance to assay for enzyme X? Would the absorbance increase or decrease over time? B.)If Vmax = 60 μmol/min and you used 400 μL of a 0.1 mg/mL solution of enzyme, what is the turnover number?Calculate the volume of BSA stock that will be required to make the standard solutions needed to create the BSA standard curve. Be sure to show your work and include the volume of 0.02 M phosphate buffer required to reach a final volume of 1 mL. From a 2,000 μg/mL BSA stock, create 1 mL of each of the following stock solutions in 0.02 M phosphate buffer using individual microcentrifuge tubes: 50 μg/mL, 250 μg/mL, 500 μg/mL, 1,000 μg/mL, 1,250 μg/mL, 1,500 μg/mL. Be sure to properly label all the microcentrifuge tubes before creating the standards.
- You are performing an enzyme reaction that works the same way as your wheat germ acid phosphatase (WGAP) assay. First, you dissolve 10.0 umol of product into 1.00 ml of buffer, and measure an absorbance of 0.500. Your cuvette has a 1.00 cm pathlength. Next, you perform the enzyme assay. Your enzyme solution has a concentration of 20.0 ug/ml. 1) Mix 0.250 ml substrate buffer with 0.250 ml enzyme 2) Incubate 20.0 min 3) Stop the assay with 0.500 ml NaOH 4) Read an absorbance of 0.200 *The units required for each answer in this problem are given. Answers to all three parts should be rounded to a maximum of three decimal places. Do not enter any letters. What is the extinction coefficient (ml/umol/cm) of the product? What is the catalytic activity (umol/min) measured in your assay? What is the specific activity (umol/min/ug) measured in your assay?The standard curve to determine the amount of betacyanin is shown below. You extracted a red pigment from a beet disc (the mass of a disc is 2 g) using 10 ml of 20% ethanol solution. You measured absorbance of the solution above the beet disc every minute for a total time of 20 minutes. The increase in absorbance was linear during a period of time from 1 min to 10 min. The absorbance at 10 min was 0.8. Calculate the amount of betacyanin extracted from 1g of a beet tissue per minute. Explain your calculations. You can use Excel or a calculator.A 0.5 M phosphate buffer at pH 6.5 and a 10 mM substrate stock solution are available for preparing enzyme assays. Each assay must have a total volume of 3 mL and a final phosphate concentration of 100 mM is desired. Using the substrate concentration of 3.33 mM and 100 µL of the enzyme solution, calculate the volume of buffer, volume of substrate stock solution, and volume of water that should be place in a cuvette for the assay.