Give two advantages and two disadvantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nm
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Give two advantages and two disadvantages to using the biuret reaction to measure protein
concentration compared to measuring the protein absorbance directly at 280 nm
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- Give two advantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nm.give two disadvantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nm.Give two benefits of utilizing the biuret reaction to assess protein concentration over directly measuring protein absorbance at 280 nm.
- When comparing the biuret reaction to measuring protein absorbance directly at 280 nm, list two benefits of utilizing the biuret reaction to quantify protein concentration.Answer the following questions about protein concentration determination. a) At what wavelength should an albumin protein solution placed in a quartz cuvette be measured in the spectrophotometer? Why is that? b) With which methods other than spectrophotometer can the amount of protein be measured quantitatively?Calculate the Km of the enzyme with these parameters. kcat = 130s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM
- Table 1 - Comparison of the effect of catechol concentration on the amount of product formed. Absorbance Potato extract Absorbance 0 mins after 30mins (2nd reading) (mL) 1st reading 1 Tube # la blank 2a 3a 4a 1 1 1 dH₂O Catechol (mL) (mL) 7 5 3 1 0 2 4 6 0.00 0.060 0.033 0-05-2 Q4) Give 2 reasons for adding dH₂O to these tubes in Table 1? Time for reading: 3:21 -0.11 Absorbance: Time for reading: 3.36 Q5) Tube la serves as a control, but why is this control needed? Absorbance: 0.197 Time for reading: 3.37 Based on the data from Table 1 answer these questions: Q1) What is the name of the enzyme found in potato extract? Answer: catechol Q2) What is the substrate? Answer: THO Q3) Name of product of this enzyme catalyzed reaction? Answer: Absorbance: 0.152 Time for reading: 3:39 Absorbance: . 166 ness Catechol Benzoquinone Subtract 1st from 2nd reading -0.01 0-137 0.11.19 0.119 Q6) Notice that your 1st absorbance reading in tubes 2a-4a are quite similar but it then becomes very different…A series of standard proteins and an unknown enzyme were studied by gel filtration on a Sephadex G200 (the 200 refers to the maximum pore size in kDa) column. The elution volume Vel for each protein is given in Table 1 below. (a) Plot the data in the form of log Mr versus elution volume. From the line of best fit through the points for the standards, determine the Mr of the unknown enzyme. Explain why ferritin and ovomucoid behave anomalously. Table 1 - The Vel versus Mr data Protein Mr Vel (mL) Blue dextran* Lysozyme Chymotrypsin Ovalbumin Serum albumin Aldolase Urease Ferritin# Ovomucoid# Unknown 1,000,000 14,000 25,000 45,000 68,500 150,000 500,000 700,000 28,000 ⎯ 85 200 190 170 150 125 90 92 160 139 *Blue dextran is not a protein but a high-Mr carbohydrate that has a covalently bound blue dye, and it elutes with the void volume of the column. # Do not…The absorbance values for different BSA standards. How can the protein concentration be calculated? Which absorbance value should be used?
- A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).In quantitative determination of protein using spectrophotometer how can I plot the absorbance vs wavelength for the proteins given the transmittance values?Calculate protein concentration in unknown samples 1, 2, 3: Absorbance of Unknown 1 = 0.541 Absorbance of Unknown 2 = 0.85 Absorbance of Unknown 3 = 1.02 Standard Curve: Y = 0.0073x