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.
Highlights
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
Sorbtion of dipeptides on AV-17-8 is higher in comparison with their monomeric amino acids
Summary
Треонилтреонина и их мономерных аминокислот лейцина и треонина анионитом АВ-17 и катионитом КУ-2-8 в широком диапазоне равновесных концентраций. Что наличие гидрофильных ОН-групп в молекуле треонина способствует сверхэквивалентной сорбции треонина на катионите. Наличие ОН-групп в боковой цепи дипептида практически не влияет на сорбцию на КУ-2-8. Сорбция дипептидов на АВ-17-8 выше по сравнению с их мономерными аминокислотами. Ключевые слова: сорбция, дипептид, аминокислота, анионит, катионит Для цитирования. И. Сорбция дипептидов и аминокислот ионитами / З.
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