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 concentrations you would calculate for samples Unknown A and Unknown B? Briefly explain your answer.
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- Mass spectrometry is an extremely versatile detection system for GC. However, interfacing an HPLC system to a mass spectrometer is a much more difficult task. Describe the major reasons why it is more difficult to combine HPLC with mass spectrometry than it is to combine GC with mass spectrometry.You obtained the following raw data when setting up a Biuret standard curve: Absorbancy 540nm BSA (mg/ml) 0.158 1 0.210 2 0.260 3 0.305 4 0.360 0.410 0.455 7 0.510 8 0.530 9 0.550 10 0.554 After blanking against a biuret-dH20 sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.279 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).SPECTROPHOTOMETRY 1.) Slope of regression line or Molar absorptivity (µM -1cm-1) is 0.0253 and absorbance of unknown solution is 0.131. What is the concentration of the unknown solution (µM )?
- In 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 calculationIn spectrophotometric analysis, the relationship between the absorbance A and the analyte's concentration C is: A = ebC + Ablank What is the molar extinction coefficient I and its absolute uncertainty if A is 0.68 ± 0.06; Ablank is 0.06 ± 0.01; b is 1.00 cm; and C is (0.45 ± 0.03)x10-5 mol/L?Q5. Figure 2 shows the mass spectrum of the same compound from an El source and a Cl source. (a) Which mass spectrum would be best for determining the molecular mass of the compound? Why? (b) Which mass spectrum would be best for determining the chemical structure? Why? (c) The El source was a pulsed source used with a TOF mass analyzer. If the flight tube were 1.0 m long and the accelerating volt age were 3000 V, what would the flight time be for the ion at m/z = 58? Relative abundance 100 80 60 40 20 0 T 50 58 69 ul 100 m/z 150 200
- 3. The lead in a swab sample, lead standards, together with a blank were made up in 5.00 mL volumetric flasks using 0.2 % HNO3. 20 μL aliquots of these solutions were injected into the spectrophotometer and the absorbance measured at 217 nm. The following results were obtained. lead / ppb Absorbance 0 0.0591 10.00 0.0858 50.00 0.1926 100.0 0.3260 150.0 0.4594 200.0 0.5929 Swab sample 0.3700 (a) Determine the amount of lead in the swab sample in μg.A juice concentrate was colorimetrically assayed using Nelson’s test. One milliliter (1.00 mL) of the sample solution and various concentrations of the standard glucose solution were treated with freshly prepared Nelson’s reagent and arsenomolybdate reagent and then diluted to 10.0 mL separately in properly labeled test tubes. Absorbances at 480 nm for distilled water, glucose standard, and for the sample are 0.052, 1.702, and 0.926, respectively. What is the reducing sugar concentration (mg/mL) in the juice concentrate? The equation of the line was plotted to be: y = 1.6656x - 0.0885 0.578 mg/mL 577.9 mg/mL 57.7 mg/mL 5.78 mg/mLA spectrophotometric method for the quantitative analysis of Fe2+ in blood uses Zn2+ as an internal standard. A sample containing Fe2+ and Zn2+ with final concentration of 3.25 ppb and 0.75 ppb, respectively, that yields a signal of 0.423 for Fe2+ and 0.650 for Zn2+. Subsequently, a sample of blood is spiked with Zn2+ to give the same final concentration and yielded a signal of 0.832 for Zn2+ and 0.110 for the unknown concentration of Fe2+. Determine the concentration of Fe2+ in the sample of blood.
- A student weighed out 0.150 g of protein powder and dissolved it in 100 mL of water (Solution 1). The student then diluted this solution by transferring 1 mL into a 25 mL flask and diluting with water (Solution 2). Finally, 1 mL of that solution was transferred to a test tube and combined with 4 mL Bradford reagent. The absorbance of the solution in the test tube was 0.144. Assuming that the best fit linear line of the standard curve was y=0.04144x+0.01521 (μgmL), calculate the percent protein by mass in the original protein powder.A solution is prepared by diluting 2.79 mL of the blue dye stock solution to 25.00 mL. The measured absorbance for the prepared solution is: Blue dye stock solution = 0.293 M Absorbance at 630 nm = 0.00265 Calibration curve y = 0.0833x A.) What is the theoretical molar concentration? B.) What is the experimental molar concentration? C.) What is the percent error?a 50.00-mL sample containging an analyte gives a signal of 11.5(arbitrary units). A second 50-mL aliquot of teh sample, which is spiked with 1.00-mL of a 10.0-ppm standard solution of the analyte, gives a signal or 23.1. what is the concentration of analyte in the original sample?