We completed a lab with the following instructions: Part B: Setting up a standar

Question

We completed a lab with the following instructions: Part B: Setting up a standard curve Part B: Setting up a standard curve 1. Warm up the Spectrometer at 595 nm 2. Set up nine large, clean test tubes to use for the assays. 3. Set up protocol as below using the most accurate pipette available, pipette the BSA standard into the tubes. The protein concentration is very high, and the volume is low, so any pipetting error will lead to poor standard curves. Reagent/tube (mL) 1 2 3 4 5 6 7 8 9 BSA Standard 1mg/ml (uL) 0 10 20 30 40 50 75 100 0 Unknown Protein 0 0 0 0 0 0 0 0 50 Bradford Reagent 3ml 3ml 3ml 3ml 3ml 3ml 3ml 3ml 3ml 4. Obtain an unknown BSA solution. Choose volume of the unknown to assay and pipet into tube 9. Must be less than 100ul. 5. Add 3ml Bradford reagent to each tube. Vortex immediately after adding the reagent to each tube. Do not wait until you have added it to all tubes. 6. Let the tubes sit about 10min before reading the absorbanciers. Once the color develops, is is stable for over an hour. 7. Make a plot to determine how much BSA you can add without the curve straying from linear. Our lab results BSA Absorbancy 0 1.798 10 1.857 20 1.926 30 2.059 40 2.146 50 2.286 75 2.465 100 2.448 Unknown 2.244 I have to do a BSE standard curve and a log curve as well. I am not sure how to do this? PLEASE HELP ME! I tried doing my Absorbency as Y and BSA concentration as X but my curve looks off. Could just mean we got bad results too? Also we have to find the concentration of our unknown? we added 50ul of the unknown. I'm soooo confused at this point and when i ask my professor he is not any help.

Explanation / Answer

this pdf file cntain your answer pl read it and rate me pl [PDF] Measuring Protein Concentration through Absorption ... www.marietta.edu/~spilatrs/biol309/.../Spectrophotometry.pdf

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