A review of an experiment that utilized gel filtration chromatography in the separation of protein biomolecules.
Written in 2009; 2,836 words; 8 sources; MLA; $ 84.95
Paper Summary:
The paper explains that gel filtration chromatography utilizes the physical properties of molecular size and shape to attain a separation of proteins. A table that summarizes the properties of several gel filtration media and a graph that estimates the extracted proteins' molecular weights are presented and the paper describes the experiment where separate solutions of protein standards and extracts were subjected to gel filtration chromatography. The chromatographic set-up and the applications of gel filtration chromatography are also discussed.
Outline:
Abstract
Discussion of Data and Results
From the Paper:
"Chromatography is a separation method that takes advantage of the relative rates at which chemical substances in a mobile phase are retained on a stationary phase. Classification of the various chromatographic techniques are based on factors including state of retaining material, nature of retaining force and mobile phase, method of termination and solute introduction, and presence or absence of gradients [1]."
Gel filtration chromatography, also known as gel permeation, gel filtration, molecular sieve or molecular exclusion chromatography, utilizes the physical properties of molecular size and shape to attain separation. In this method, the stationary phase consists of inert gel bead particles with small pores of controlled size and porosity [2]."
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