title: Multiple peak formation of avidin on an iminobiotin affinity support.
abstract: When pure avidin is chromatographed on a homemade iminobiotin column, two distinct peaks are observed using a gradient solvent system starting with a pH 9 buffer. Proteins in both peaks are shown to be identical by nondenatured polyacrylamide gel electrophoretic experiment. The weak interaction of the protein with the stationary phase at pH 9 could cause this unusual behavior.
authors.affiliation: Department of Chemistry, Box 9573, Mississippi State University, Mississippi State, MS 39762, USA. TL45@ra.msstate.edu
authors.forename: Yan
authors.initials: Y
authors.lastname: Wang
authors.forename: Tingyu
authors.initials: T
authors.lastname: Li
mesh_terms: D001360:Avidin / Q000032:analysis*; D001710:Biotin / Q000737:chemistry*; D002846:Chromatography, Affinity / Q000295:instrumentation*; D004591:Electrophoresis, Polyacrylamide Gel
chemical_list: D001360:Avidin; D001710:Biotin