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Please help me answer and explain these questions:
1. Compare the abundance of A280 chromophores (W, Y, and C) to Bradford sites (loosely R and K) in BSA.
2. We used a protocol that corrects the path length in each well and normalizes the absorbance to the value that would be obtained if the path length were 1 cm (the standard path length). Using this observation and your A280 calibration data, what is your measured e280, for BSA?
Answer :
Q1. Advantage absorbance at 280 nm : It is very simple. Also the sample is not destroyed
Disadvantage is of interference from nonprotein chromophores.
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- Standard curves You are setting up a standard curve for lysozyme. You have a stock vial containing 2 mg/ml of lysozyme and you have 2 ml in the vial. You will want to have a minimum of 1 ml of each concentration for the spectrophotometer. How would you proceed? (Saline is added to make the various concentrations). Concentration Am't stock lysozyme or am't of a previous dilution (note which) Amount saline Total volume wanted 1.00 mg/ml 0.75 mg/ml 0.50 mg/ml 0.375 mg/mlVarious concentrations of recombinant human insulin were prepared for use standards for an HPLC method. To verify the prepared concentrations, the samples were analyzed by measuring the absorbance at 280 nm in a short path length (5 mm) cuvette. The molar absorption coefficient for human insulin is approximately 5.875 x 10³ M-¹cm-¹. a. Calculate the extinction coefficient in mL mg-¹cm-¹. b. Calculate the concentrations of the following human insulin standards if the measured absorbances and dilutions used are: Standard 1 Standard 2 Abs. (at 280 nm) of Diluted Sample 0.305 0.685 Dilution 145.0 µL sample, 25.0 μL buffer 130.0 µL sample, 40.0 μL bufferDuring a mass spectrometry experiment, the spectrum of vascular endothelial growth factor A (VEGF-A) was acquired. The absolute error of VEGF-A, having a mass of 1024.5210 Da was 0.06 Da. Calculate the relative error (ppm).
- Theoretical Data Following the modified protocol for the isolation of Escherichia coli bacteriophage of Encabo (2018) presented below, compute for the pfu/ml of the chloroform-treated lysate. 1ml 1ml 1ml 1ml 1 Chloroform-treated lysate 1ml Dilution 10-3 10-4 10-5 0 0 0 0 0 9ml 9ml 9ml 10-1 10-² 10-3 Empty sterile tubes Incubate inside ref for 15-20min + 0.1 ml lysate-E.coli mix 0.1 ml 9ml 9ml 104 10.5 // 0.1 ml 0.1 ml +0.5 ml E. coli ↓↓↓↓↓↓ Incubate O/N at 35°C, observe for plaques Molten soft agar overlay B. Quantification of the Infective E. coli other Bacteriophage Particles in the Raw Sewage Sample Volume of Stock Plated (in ml) Bottom agar No. of Plaque-Forming Units (pfu) Ave. A B 254 265 132 110 11 23For 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 are the initial concentrations used for tubes 3, 5, and 6? Show pertinent solutions. What are the dilutions of the last positive tube and first negative tube respectively? Show computation.In basic spectrophotometer, 1. Calculate the concentration of bovine serum albumin (BSA) if 40% of a light beam is transmitted through 2 cm of the cuvette (assume the molar absorption coefficient, e is 43,824 M-1 cm-1). 2. Calculate the %T, if the concentration of BSA in a 2 cm of cuvette is 0.025 mg/mL. and compare between 1 and 2