Analytical separation of amino acids on a cation-exchange resin cross-linked with m-divinylbenzene.
The elution bands of acidic and neutral amino acids of protein hydrolysates, emerging from the column of a cation-exchange resin cross-linked with pure m-divinylbenzene, are narrower than those from a resin prepared from styrene and technical divinylbenzene. As a result of these narrower bands, a more complete resolution of the critical pairs threonine-serine, glycine-alanine and tyrosine-phenylalanine is obtained. The most probable reason for the narrower elution peaks is the more rapid diffusion of the exchanged components through the bulk of the resin as a result of a more regular arrangement of cross-linkages in the cation-exchange resin prepared from m-divinylbenzene.
Analytical separation of amino acids on a cation-exchange resin cross-linked with m-divinylbenzene. The elution bands of acidic and neutral amino acids of protein hydrolysates, emerging from the column of a cation-exchange resin cross-linked with pure m-divinylbenzene, are narrower than those from a resin prepared from styrene and technical divinylbenzene. As a result of these narrower bands, a more complete resolution of the critical pairs threonine-serine, glycine-alanine and tyrosine-phenylalanine is obtained. The most probable reason for the narrower elution peaks is the more rapid diffusion of the exchanged components through the bulk of the resin as a result of a more regular arrangement of cross-linkages in the cation-exchange resin prepared from m-divinylbenzene.