Abstract
The chromatographic characteristics of 13 polypeptides were studied on home-made layers of silanized silica gel alone and impregnated with N-dodecylpyridinium chloride and also on RP-2 plates. The influence of the type and percentage of organic solvent, of the pH and ionic strength of the eluent and of the percentage of detergent on the layer was investigated. Attempts were made to understand the retention mechanism of the polypeptides in relation to their molecular weight, charge and structure. Hydrophobic and electrostatic interactions are responsible for the chromatographic behaviour of the different compounds. Separations of five actinomycins, of angiotensins and of other polypeptides were carried out on RP-2 plates and on layers of silanized silica gel impregnated with N-dodecylpyridinium chloride.
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