title: Interactions and compatibility of 11 S globulin from Vicia faba seeds and sodium salt of carboxymethylcellulose in an aqueous medium.
abstract: This work studies specific interactions and compatibility between a legumin and a linear carboxylated polysaccharide using gel permeation chromatography, sedimentation analysis, SDS gel electrophoresis, viscometry and phase analysis measurements. It uses the system water/11 S globulin/CMC as a model. Carboxymethylcellulose (CMC) molecules are able to cause a partial dissociation of the protein, subsequent formation of soluble interbiopolymeric complexes and partial aggregation of the free non combined protein at room temperature and pH 6.0-6.5. The maximal binding of biopolymers is observed at their equimolar ratio. The decrease in temperature of the mixture from 293 to 277 K leads to formation of the complex coacervate. The increase in pH from 6.0 to 7.6 results in suppression of complex formation and manifestation of the phenomenon of thermodynamic incompatibility if the total concentration of biopolymers in the system exceeds the critical concentration of segregative phase separation.
authors.affiliation: N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Kosigin Str. 4, 119991 Moscow, Russia. chehonter@yandex.ru
authors.forename: Yu A
authors.initials: YA
authors.lastname: Antonov
authors.forename: A P
authors.initials: AP
authors.lastname: Dmitrochenko
authors.forename: A L
authors.initials: AL
authors.lastname: Leontiev
mesh_terms: D002266:Carboxymethylcellulose Sodium / Q000737:chemistry*; D002847:Chromatography, Agarose; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D010940:Plant Proteins / Q000737:chemistry*; D011485:Protein Binding; D012996:Solutions; D031307:Vicia faba / Q000737:chemistry*; D014783:Viscosity; D014867:Water
chemical_list: D046911:Macromolecular Substances; D010940:Plant Proteins; D012996:Solutions; D014867:Water; D002266:Carboxymethylcellulose Sodium