Question

can anyone help me? see the picture below

Answer 1

@thomaster

Answer 2

@wolfe8

Answer 3

@whpalmer4

Answer 4

Looks like fun, but after a few minutes of searching, I have yet to find a description of the process that I can decipher!

Answer 5

This is easy,

\[\frac{BSA_{Abs}}{BSA_{Conc}} = \frac{Protein_{Abs}}{Protein_{conc.}}\]

Or you could create a line of best fit and use that to determine the protein concentration.

We are assuming in this experiment that the enzyme of interest absorbs proportionally to the BSA. It is just a quick way of measuring protein concentration.

Answer 6

This is a pretty cheap and quick method (but not the most accurate). You will want to use the point with the absorbance closest to the absorbance you obtained for the enzyme for the equation I posted above

Answer 7

@whpalmer4 can you help me? I am not sre if I get his point

Answer 8

Why not just ask if you do not understand

Essentially from the graph you can either:

Use linear or non-linear regression (probably the best way to go about this but it doesn't really seem like an option for this question) and generate a function characteristic of the calibration curve.

Or

You can use the formula I provided and use the point (0.4, 20micrograms) and sub it into the formula I provided which basically states that the absorbance is proportional to that of the concentration and that the molar absorptivity (the ability for a substance to absorb electromagnetic radiation) of BSA is proportional to that of the enzyme of interest.

https://en.wikipedia.org/wiki/Beer%E2%80%93Lambert_law
https://en.wikipedia.org/wiki/Molar_absorptivity

Answer 9

So you would just be solving for Protein_amount you have all the other variables then you can go on to figure out concentration

that formula should have variables with the subscript amount not concentration