Enzymatic deglycosylation of glycoproteins

Min Sung Kim, Dan Leahy

Research output: Chapter in Book/Report/Conference proceedingChapter


Recombinant protein expression using eukaryotic expression systems has certain advantages, such as addition of posttranslational modifications that help protein stability and activity. Asparagine-linked sugar attachment is one of the most common posttranslation modifications. However, sugar modification can impede the growth of high-quality protein crystals for structural studies using X-ray crystallography. To overcome this problem, consensus sites of N-linked attachments can be mutated into other similar residues, such as aspartic acid. Alternatively, enzymatic deglycosylation can be used to remove sugars. Peptide-N-Glycosidase F (PNGase F; EC and Endoglycosidase H (Endo H; EC are the most popular enzymes for this purpose.

Original languageEnglish (US)
Title of host publicationLaboratory Methods in Enzymology
Subtitle of host publicationCell, Lipid and Carbohydrate
PublisherAcademic Press Inc.
Number of pages5
ISBN (Print)9780124200678
StatePublished - Jan 1 2013

Publication series

NameMethods in Enzymology
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988


  • Affinity purification methods
  • Enzymatic deglycosylation
  • Glycoproteins
  • Maltose-binding protein (MBP)
  • Oligosaccharides
  • Recombinant proteins

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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