Abstract
The merits of hydrophobic interaction chromatography on octyl-Sepharose as a method for the separation of carrier ampholytes from peptides have been investigated. K values for the association of octyl groups with small model peptides and with carrier ampholytes in aqueous sodium chloride-containing phosphate buffers were determined as a function of ionic strength and pH. A separation of a somatomedin-containing peptide mixture into seven fractions by hydrophobic interaction chromatography on octyl-Sepharose is shown.
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