title: Protein binding of procyanidins: studies using polyacrylamide gel electrophoresis and French maritime pine bark extract.
abstract: The application of PAGE to determine the interaction between procyanidins and proteins, as presented here, enables one to directly determine the binding of either a pure of a complex mixture of flavonoids to a particular protein. If the protein of interest is an enzyme, the combination of PAGE with quantitative activity measurements allows identifying whether a change in the enzyme activity is related to the binding. Data presented suggest that PBE and EGb 761 have protein-binding properties, which, in addition to their redox-based effects, could provide a biochemical basis for their action in biological systems.
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3200, USA.
authors.forename: H
authors.initials: H
authors.lastname: Moini
authors.forename: Q
authors.initials: Q
authors.lastname: Guo
authors.forename: L
authors.initials: L
authors.lastname: Packer
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel; D010936:Plant Extracts / Q000737:chemistry*; D011485:Protein Binding; D014197:Trees / Q000737:chemistry; D014969:Xanthine Oxidase / Q000378:metabolism
chemical_list: D010936:Plant Extracts; D014969:Xanthine Oxidase