Sorption of peptides and amino acids by ion exchangers

Abstract

Sorbtion of dipeptides leucylisoleucine, threonylthreonine and their monomeric amino acids leucine and threonine by anionite AV-17 and cationite KU-2-8 in a wide range of equilibrium concentrations has been studied. It was shown that the presence of hydrophilic OH-groups in the threonine molecule promotes superequivalent sorbtion of threonine on the cation exchanger. The presence of an OH-groups in the side chein of the dipeptide practically does not affect the sorbtion an KU-2-8. Sorbtion of dipeptides on AV-17-8 is higher in comparison with their monomeric amino acids.