Literature DB >> 23695958

Size fractionation of microscopic protein aggregates using a preparative fluorescence-activated cell sorter.

Verena Rombach-Riegraf1, Cyril Allard, Eline Angevaare, Anja Matter, Bahman Ossuli, Rene Strehl, Friedrich Raulf, Markus Bluemel, Kamal Egodage, Margit Jeschke, Atanas V Koulov.   

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.
Copyright © 2013 Wiley Periodicals, Inc.

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Year:  2013        PMID: 23695958     DOI: 10.1002/jps.23532

Source DB:  PubMed          Journal:  J Pharm Sci        ISSN: 0022-3549            Impact factor:   3.534


  2 in total

1.  Comparative Evaluation of Two Methods for Preparative Fractionation of Proteinaceous Subvisible Particles--Differential Centrifugation and FACS.

Authors:  Björn Boll; Emilien Folzer; Christof Finkler; Jörg Huwyler; Hanns-Christian Mahler; Roland Schmidt; Atanas V Koulov
Journal:  Pharm Res       Date:  2015-07-21       Impact factor: 4.200

2.  Physical characterization and in vitro biological impact of highly aggregated antibodies separated into size-enriched populations by fluorescence-activated cell sorting.

Authors:  Srivalli Telikepalli; Heather E Shinogle; Prem S Thapa; Jae Hyun Kim; Meghana Deshpande; Vibha Jawa; C Russell Middaugh; Linda O Narhi; Marisa K Joubert; David B Volkin
Journal:  J Pharm Sci       Date:  2015-03-05       Impact factor: 3.534

  2 in total

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