In case of compound proteins (e.g. Glycoproteins), how is the protein separated to study its function?
To study the function of a protein; it must be separated it in the functioning active form meaning that it must be purified with the carbohydrate residues attached: via applying the protein mixture to an affinity chromatography column and purify it then to study its function by the specified methods for such a protein. Q15. During salting out, by adding more salts, proteins tend to combine with each other and concentrate – How do the amino acids of a certain protein will precisely concentrate with each other at certain solution saturation (e.g. fibrinogen at 1/4 saturation)? A:During salting out, the precipitate at a certain concentration that the precipitated proteins wouldn’t mix. For example: At 1/4 concentration ammonium sulfate, fibrinogen precipitates. Then you transfer the supernatant to a new container so you have the fibrinogen precipitate. Then, you increase the concentration till globulin precipitates. You transfer the supernatant to a new clean container; so you’d have the
