Open AccessSorption of peptides and amino acids by ion exchangers
Author(s) -
З. И. Куваева,
E. G. Karankevich
Publication year - 2021
Publication title -
vescì nacyânalʹnaj akadèmìì navuk belarusì. seryâ hìmìčnyh navuk
Language(s) - English
Resource type - Journals
eISSN - 2524-2342
pISSN - 1561-8331
DOI - 10.29235/1561-8331-2021-57-3-278-285
Subject(s) - dipeptide , amino acid , monomer , chemistry , threonine , leucine , sorption , peptide , ion exchange , stereochemistry , ion , organic chemistry , biochemistry , serine , enzyme , polymer , adsorption
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.