A typical chromatogram shows an initial broad peak of eluted protein that only occasionally or never interacts with the resin. The column is typically rinsed with binding buffer until the A280 reading returns to baseline and this first flowthrough peak has completely eluted. Then, by altering the elution buffer's composition, proteins that have a strong interaction with the resin are removed. The physicochemical characteristics of the molecules to be separated and the Liquid Chromatography Market media being used often referred to as various media chemistries—determine the precise composition of the elution buffer. Elution buffers of increasing ionic strength are used in ion exchange chromatography, for instance, which depends on interactions based on the net charges of the molecules.
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