You put 50 uL of 0.1 mg of protein into a 1 cm pathlength cuvette containing 3 mL of LDH reaction mixture and measure a slope of 0.125 abs/min in an LDH assay. What is the reaction rate in uM/min? Show your work.
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- Using a P-1000 micropipette, you transfer 800 microliter of ddH2O to a beaker and measure its weight. It turns out to be only 780 milligram; what is the percent error of this micropipette?Calculate the amount of protein (in mg) in Sample 1 if the measurement at A280 = 0.197, taking into account the dilution factor 100 per and total volume of extract 140mlWhat is the change in concentration (umol/mL/min) for NADPH if the change in absolute absorbance per second from your DHFR functional assay analysis was 0.0035?
- If I had a standard with 2.0 mL of Bradford reagent then added 50μL of 250 μL/mL ; what would be the concentration of original protein?I need to prepare a standard calibration curve for gamma globulin. absorbances on Y and mg of standard protein per assay on X. used 0.1mg/ml gamma stock for tubes 2-6. (Water (ml), gamma (ml), Abosrbance)--> (.036, .004, .290) (.036, .008, .358) (.024, .016, .341) (.016, .024, .520) (.008, .032, .597) - What is the math and how do you get the standard curve?You obtained the following raw data when setting up a Bradford standard curve: BSA (mg/ml) Absorbancy 595nm 0 0.225 1 0.310 2 0.420 3 0.510 4 0.610 5 0.720 6 0.810 7 0.915 8 0.950 9 0.980 10 0.990 After blanking against a bradford-dH2O sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.570 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).
- 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)What is your overall dilution factor if you complete 3 serial dilutions using a 100-fold dilution each time? (Show your work)Calculate the amount of protein (in mg) in Sample 1 if the measurement at A280 = 0.636, taking into account the dilution factor as per question 6 (100ul) and the total volume of extract as per question 4 (140ml). Give your answer as a number with no decimal places.
- You are given as following : 20 µl pure LDH on ice, 2.0ml of 6mM NAD+, 2.0ml of 150mM lactate, and 0.14M CAPS buffer. LDH reaction cocktail has final concentration of 1mM NAD+ and 25mM lactate in 0.14M CAPS buffer. LDH activityis measured by mixing 10 µl of LDH sample and 990 µl LDH reaction cocktail before getting ∆A340/min reading on spectrometer. (a). Describe in detail how you would prepare for your LDH reaction cocktail including how to make dilutions.Based on this video https://www.youtube.com/watch?v=rKng5-ij6kQ Provide a schematic diagram for the Iodine test methodologies in determining the presence of carbohydrates. Also, give the basic principle for the test.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?