HPLC: Boronate Affinity Chromatography of Glycopeptides

Apffel, Alex (alex_apffel@hpl.hp.com)
Tue, 16 Mar 1999 09:15:34 -0800

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We are trying to use boronate affinity columns from TosoHaas to isolate
glycosylated recombinant proteins and glycosylated peptide fragments
produced upon proteolytic digestion of the recombinant glycoproteins. These
are primarily, but not exclusively N-linked glycosylation. As an
alternative to Lectin Affinity chromatography, the use of the boronate
columns sounds attractive because we could simultaneously isolate N- and
O-linked glycopeptides from non-glycosylated peptides and elute the
fractions in mobile phases that are relatively friendly to subsequent LC/MS
and CE/MS analysis. A suggestion has been made that boronate columns work
well for glyco-amino acids, less well for glycopeptides and poorly for
glycoproteins. Can you shed some light on this for us.

Alex Apffel, Ph.D.
Biomeasurements Group
Hewlett-Packard Laboratories
3500 Deer Creek Road
Palo Alto, CA 94304 USA
Tel 650-857-6090
Fax 650-852-8502
email alex_apffel@hpl.hp.com

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