Protein purification: size-exclusion chromatography

In this specific lab, we used a purification method, Gel filtration chromatography, to separate a mixture of two molecules known as Blue Dextran and Fluorescein based on the size of the molecule. A column was prepared using a gel filtration medium called Sephadex G-50. Prior to class Dr.Regmi made an elution buffer of Na2HPO4/ NaH2PO4 pH 7.0 for size-exclusion chromatography.

Through the duration of this lab, I learned that the atoms that are bigger in size normally elute the section first before more modest particles can, due to their exchanges with the fixed stage, the beads.

Below is a list of a variety diameters of organelles; this determines the RCF required


Below is a video of the Gel-filtration Sephadex G-50 Procedure



Comments

  1. Hey, thank you for adding the picture of the diameters of the organelles. that was lab was interesting to see how chromatography worked in real life. I also appreciate you putting a video that explains the procedure of the lab. Thank you for your contribution to this topic.

    ReplyDelete

Post a Comment

Popular posts from this blog

The Basics of SDS - PAGE

Buffers

Determination of Protein Concentration: Spectrophotometry