endoglycosidase


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endoglycosidase

[‚en·dō·glī′kō·sə‚dās]
(biochemistry)
An enzyme which releases intact glycans from their linkages with amino acids.
References in periodicals archive ?
Oxurion added that heparanase is an endoglycosidase that is important in modifying the extracellular matrix and in inflammatory processes.
For deglycosylation of the recombinant endo-[beta]-1,4-glucanase, ten micrograms of recombinant enzyme were incubated with 100U of endoglycosidase H (Endo-H) at 37[degrees]C for 1 h.
For example, various N-glycans were transferred from the corresponding oxazolines to the GlcNAc residue on the intact anti-Her2 antibody with a mutant endoglycosidase, affording glyco-engineered anti-Her2 antibodies (Fig.
WFS1 gene encodes wolframin, an endoglycosidase H-sensitive transmembrane glycoprotein localized in the endoplasmic reticulum (ER).
The treatment of cell-free extracted HA with endoglycosidase PNGase F that removes N-linked glycosyl chains from a peptide backbone revealed two distinct bands in Figure 2(a).
HPSE is the sole human endoglycosidase that cleaves HS, although this molecule also displays various nonenzymatic activities [16, 17].
PG545 is a heparan sulphate mimetic that inhibits heparanase, the only endoglycosidase which cleaves heparan sulphate chains in the ECM [49, 50].
Studies from our laboratory also revealed the majority of breast cancer cell lines harbor differential glycosylation patterns (specifically in the secreted pro-CatD), with prevalence of endoglycosidase H (EndoH) sensitive N-glycan structures (Figure 2 B and 2C, Khalkhali-Ellis, unpublished observations) [47].
Maeda et al., "Molecular cloning and gene expression analysis of tomato endo-[beta]-n-acetylglucosaminidase, an endoglycosidase involved in the production of high-mannose type free N-glycans during tomato fruit ripening," Bioscience, Biotechnology and Biochemistry, vol.
First, PrP-T182A (hereafter referred to as Mut-PrP) transiently expressed for 16 h produced only non- and monoglycosylated PrP that were sensitive to Endoglycosidase H (N2a data, using 3F4 tagged PrPs is presented), supporting a lack of complex glycosylation and limited trafficking to cis-Golgi (Figure 1(a)); second, phosphatidylinositol-phospholipase C (PIPLC) treatment, which cleaves PrP from its GPI anchor, effectively released surface-bound Wt-PrP, but not Mut-PrP, into the culture media (COS-7 cell data, using nontagged PrPs, presented) (Figure 1(b)); and third, immunofluorescence confocal microscopyshowed Wt-PrP to be consistently present on the plasma membrane, whereas Mut-PrP was consistently absent (N2a data presented).
Another example is the treatment of patient sera with bacteria-derived endoglycosidase S.
Hyaluronidase is an endoglycosidase that degrades hyaluronic acid into smaller fragments.