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Q3. Which isolate has A260/280 ratio of above 2.0?
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- 50 uL of an aqueous sample of double-stranded DNA is dissolved in 950uL of water. This diluted solution has a maximal absorbance of 0.326 at 260 nm. What isthe concentration of the original (more concentrated) DNA sample, expressed in ug/ul? I would like to know the process of this question. And I was wandering as well if the total diluted volume would be 950ul + 50ul = 2000ulIn a Bradford assay, 17 pl of a protein isolate sample was diluted by adding 24 pl of water prior to the addition 2.0 mL Bradford reagent, Calculate the protein concentration (in mg/ml) of the original protein isolate sample whose absorbance reading at 595 nm is 0,384 after dilution The protein standard solutions used for the calibration curve of the Bradford assay was constructed using bovine serum albumin (BSA) stock solution whose concentration is 200 ug/mL The concentration and the corresponding absorbance reading at 595 nm of the protein standard solutions are summarized in the table below: Standard soln # 3 6 conc of BSA Kug/mL) 12.00 24.00 36.00 48.00 60.00 Absorbance lat 595 nm 0.000 0.156 0.249 0.328 0.411 0.528 zNote: Final answer format must be x.xox (three decimal places) Round off only in the final answer. Do not round off in the middle of the calculation50 uL of an aqueous sample of double-stranded DNA is dissolved in 950uL of water. This diluted solution has a maximal absorbance of 0.326 at 260 nm. What isthe concentration of the original (more concentrated) DNA sample, expressed in ug/ul? I would like to know the process of this question. And I was wondering as well if the total diluted volume would be 950ul + 50ul = 1000ul
- The standard curve of a biuret assay gave the equation: y=0.4193x. The absorbance for Unknown A = 0.098 and Unknown B = 0.325. Are you equally confident in the accuracy of the protein %D concentrations you would calculate for samples Unknown A and Unknown B? Briefly explain your answer.The Bradford method described in the Background section was used to determine protein concentrations of known and unknown samples The following results was obtained: Table 1: Absorbance at 595nm obtained for different concentrations of protein standards using the Bradford method Protein (mg/ml) 0.00 0.125 0.25 0.50 0.75 1.00 1.50 2.00 Unknown Abs. BSA 0 0.130 0.350 0.620 0.870 1.120 1.400 1.600 0.635 Abs. BIg 0 0.080 0.230 0.460 0.520 0.410 0.510 0.700 Calculate the concentration of the unknown protein in mg/mlOne common way to determine phosphorous in urine is to treat the sample after removing the protein with molybdenum (VI) and then reducing the resulting 12-molybdophosphate complex with ascorbic acid to give an intense blue-coloured species called molybdenum blue. The absorbance of molybdenum blue can be measured at 650 nm. A 24-hour urine sample was collected, and the patient produced 1122 mL in 24 hours. A 1.00 mL aliquot of the sample was treated with Mo (VI) and ascorbic acid and diluted to a volume of 50.00 mL A calibration curve was prepared by treating 1.00 mL aliquot of phosphate standard solution in the same manner as the urine sample. The absorbances of the standards and the urine sample were obtained at 650 nm and the following results were obtained. ppm, P aBSORBANCE (A) 1.003.00 0.230 2.00 0.436 3.00 0.638 4.00 0.848 Urine sample 0.518 ffind the slope and intercept, then graph it.
- Exactly 5.00 mL aliquots of a solution containing analyte X were transferred into 50.00-mL volumetric flasks and the pH of the solution is adjusted to 9.0. The following volumes of a standard solution containing 2.00 µg/mL of X were then added into each flask and the mixture was diluted to volume: 0.000, 0.500, 1.00, 1.50 and 2.00 mL. The fluorescence of each of these solutions was measured with a fluorometer, and the following values were obtained: 3.26, 4.80, 6.42, 8.02 and 9.56, respectively. ii. Using relevant functions in Excel, derive a least-squares equation for the data, and use the parameters of this equation to find the concentration of the phenobarbital in the unknown solution.Derive an expression relating absorbance to the concentrations of standard and unknown ( c subscript s and c subscript x) and the volumes of the standards and unknown ( V subscript s and V subscript x ) as well as the volume to which the solutions were diluted (V subscript t). Derive expressions for the slope and the intercept of the straight line obtained in (a) in terms of the variables listed above.In a Bradford assay, 11 µl of a protein isolate sample was diluted by adding 21 µl of water prior to the addition 2.0 mL Bradford reagent. Calculate the protein concentration (in mg/mL) of the original protein isolate sample whose absorbance reading at 595 nm is 0.304 after dilution. The protein standard solutions used for the calibration curve of the Bradford assay was constructed using bovine serum albumin (BSA) stock solution whose concentration is 200 µg/mL. The concentration and the corresponding absorbance reading at 595 nm of the protein standard solutions are summarized in the table below: Standard soln # 1 2 13 4 6 conc of BSA 12.00 24.00 36.00 48.00 60.00 (pg/mL) Absorbance at 595 nm 0.000 0.156 0.249 0.328 0.411 0.528 zNote: Final answer format must be x.xxx (three decimal places). Round off only in the final answer. Do not round off in the middle of the calculation.
- 1. State the difference between transmittance, absorbance, molar absorptivity, and fluorescence. Which one(s) is proportional to analyte concentration?The data given below was generated by a student in Bio 240L during a Bradford Assay. A standard curve was generated by preparing a set of standard samples of protein (bovine serum albumin) and adding the dye Coomassie Brilliant Blue, When the protein binds to Coomassie Brilliant Blue it absorbed light at 595 nm with an extinction coefficient of 43,000 M-1 cm-1. After the dye binding reaction was complete, absorbance values for each protein standard solution were measured at 595 nm and recorded. Standard # 1 2 13 4 Concentration of protein binded to Coomassie Brilliant Blue (M) 6.35x10-7 1.23x10-6 3.85x10-6 5.68x10-6 OOO Absorbance at 595 nm 0.093 0.176 0.560 0.813 Prepare a standard curve with the student generated data. What is the slope from the standard curve rounded to four sig figs and no units? 1.4 143398 6.972x10-6 1.434x105A Dubosq colorimeter consists of a cell of fixed path length and a cell of variable path length. By adjusting the length of the latter until the transmission through the two cells is the same. the concentration of the second solution can be inferred from that of the former. Suppose that a plantdye of concentration 25 μg dm-3 is added to the fixed cell. the length of which is 1.55 em. Then a solution of the same dye. but of unknown concentration. is added to the second cel l. It is found that the same t ransmittance is obtained when the length of the second cel l is adjusted to 1.18 em. What is the concentration of the second solution?