title: Size fractionation of microscopic protein aggregates using a preparative fluorescence-activated cell sorter.
abstract: Protein aggregation, which takes place both in vivo and in vitro, is an important degradative pathway for all proteins. Protein aggregates have distinct physicochemical and biological properties that are important to study and characterize from the perspective of both fundamental and applied sciences. The size of protein aggregates varies across a huge range, spanning several orders of magnitude. Currently, protein aggregates larger than hundreds of nanometers in diameter are impossible to physically fractionate. Here, we present a new method to fractionate microscopic proteinaceous particles using preparative fluorescence-activated cell sorting technology.
authors.affiliation: Novartis Pharma AG, Werk Klybeck, Basel CH-4002, Switzerland. verena.rombach-riegraf@novartis.com
authors.forename: Verena
authors.initials: V
authors.lastname: Rombach-Riegraf
authors.forename: Cyril
authors.initials: C
authors.lastname: Allard
authors.forename: Eline
authors.initials: E
authors.lastname: Angevaare
authors.forename: Anja
authors.initials: A
authors.lastname: Matter
authors.forename: Bahman
authors.initials: B
authors.lastname: Ossuli
authors.forename: Rene
authors.initials: R
authors.lastname: Strehl
authors.forename: Friedrich
authors.initials: F
authors.lastname: Raulf
authors.forename: Markus
authors.initials: M
authors.lastname: Bluemel
authors.forename: Kamal
authors.initials: K
authors.lastname: Egodage
authors.forename: Margit
authors.initials: M
authors.lastname: Jeschke
authors.forename: Atanas V
authors.initials: AV
authors.lastname: Koulov
mesh_terms: D005434:Flow Cytometry / Q000379:methods*; D006801:Humans; D007074:Immunoglobulin G / Q000737:chemistry* / Q000302:isolation & purification; D008027:Light; D010316:Particle Size; D012542:Scattering, Radiation
chemical_list: D007074:Immunoglobulin G