Glycopeptidase A from almonds is used for deglycosylation. It catalyzes the removal of N-linked oligosaccharide chains and converts Asn residue to Asp.
PNGase F from
Elizabethkingia meningoseptica has been used:
- for de-N-glycosylation of Zika20virus E protein
- to evaluate coxsackievirus and adenovirus receptor glycosylation using CAR-expressing COS cells
- to verify the N-linked glycosylation of MHC class 1 polypeptide-related sequence A (MICA)
Recombinant PNGase F has been purified by affinity chromatography and dialyzed into a 50% glycerol solution with 10 mM potassium phoosphate pH 7.5 to produce a stable product. The product contains low levels of buffer salts. This highly purified material can be used for preparative deglycosylation or for analytical applications in gel, in solution, or on blot membranes. The enzyme can be removed from preparative operations by utilizing its C-terminal 6x histidine fusion tag. PNGase F from Elizabethkingia meningoseptica has been used in deglycosylation assay in human plasma samples and in deglycosylation of chondroitin sulfate proteoglycan.
PNGase F (Peptide N-glycosidase F) cleaves asparagine-linked glycoproteins, which produces carbohydrate-free peptides and detached full-length oligosaccharides.
Cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain.
