title: Electrophoretic mobility and dissociation constants of tripeptides evaluated by isotachophoresis.
abstract: Ionic mobilities and dissociation constants of twenty peptides (seventeen tripeptides and a few oligoglycines) were evaluated on the basis of the observed isotachophoretic qualitative indices RE in the pH range 8.1-9.5 by the use of a least-squares method. Good correlation was obtained among the mobilities of amino acids, dipeptides and tripeptides when the clay ball model and the conventional formula weight were adopted.
authors.affiliation: Faculty of Engineering, Hiroshima University, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Hirokawa
authors.forename: R
authors.initials: R
authors.lastname: Sugino
authors.forename: Y
authors.initials: Y
authors.lastname: Kiso
mesh_terms: D000595:Amino Acid Sequence; D004573:Electrolytes; D004586:Electrophoresis; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*
chemical_list: D004573:Electrolytes; D010455:Peptides