These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Enzymatic deglycosylation of glycoproteins. Author: Kim MS, Leahy D. Journal: Methods Enzymol; 2013; 533():259-63. PubMed ID: 24182931. Abstract: 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 3.5.1.52) and Endoglycosidase H (Endo H; EC 3.2.1.96) are the most popular enzymes for this purpose.[Abstract] [Full Text] [Related] [New Search]