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- Publisher
- Wiley
- Copyright
- Copyright © 2005 Wiley Subscription Services
- ISSN
- 0951-4198
- eISSN
- 1097-0231
- DOI
- 10.1002/rcm.1979
- pmid
- 15912476
- Publisher site
- See Article on Publisher Site
Abstract
We demonstrate a simple and rapid single‐step method to fabricate an enzyme microreactor incorporating the N‐glycosidase PNGase F (peptide‐N‐glycosidase F) into a porous polymer‐based monolith. The monolith is contained in a capillary format, while the enzyme reactor is ready to use within 1 h of preparation. The monomers making up the monolith, including N‐acryloxysuccinimide for covalent immobilization of the enzyme, are mixed with PNGase F and introduced into the column by capillary force for polymerization/immobilization. Glycoproteins (ribonuclease B, asialofetuin, α1‐acid glycoprotein, and ovalbumin) perfused through the PNGase F reactor were shown to be effectively deglycosylated on a time‐scale of seconds/low minutes using low nanogram to microgram per microliter concentration (corresponding to a total sample consumption of 0.1–20 μg of a glycoprotein). The reactor enzyme activity was shown to be reproducible for at least 8 weeks when used and stored at room temperature. Evaluation was performed by matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry. Copyright © 2005 John Wiley & Sons, Ltd.
Journal
Rapid Communications in Mass Spectrometry – Wiley
Published: Jan 30, 2005