glycosylation


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glycosylation

[glī‚käs·ə′lā·shən]
(biochemistry)
A chemical reaction in which glycosyl groups are added to a protein to produce a glycoprotein.
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References in periodicals archive ?
To be able to look at glycosylated proteins, one needs extremely high resolution hardware to distinguish the different types of carbohydrate chains (the glycosylations) with high accuracy, so there is no doubt over the nature of the glycosylation branch," explains van Gool.
Protein glycosylation is an important posttranslational modification that occurs predominantly in the endoplasmic reticulum and the Golgi apparatus.
Services in Creative BioMart include: Annotate N-linked glycosylation, Annotate O-linked glycosylation, Annotate C-linked glycosylation, Annotate glycationn, Glycan staining or labeling, Glycoprotein purification or enrichment and Glycoproteome and Glycome Analysis by Mass Spectrometry.
The main components of these compounds are glycosides that consist of a glycon part and an aglycon part connected through a glycosidic bond that can be created by a glycosylation reaction.
We applied our previously reported affinity-chromatography method in combination with a bottom-up proteomics approach comprising an enzymatic deglycosylation scheme to retain a small glycan moiety attached to the glycopeptides as direct proof of glycosylation, single as well as combined enzymatic protein digestion, [beta]-elimination with concomitant Michael addition chemistry, and high-resolution nano-LC-MS (3, 23, 24).
Sysmex has developed a reagent for testing the degree of hepatic fibrosis during blood testing, using a glycosylation marker1 developed in cooperation with AIST and building on the success of the NEDO projects,2 thereby achieving the worlds first practical realization of a system for diagnosing hepatic fibrosis using a glycosylation marker.
N-linked glycosylation in the hemagglutinin of influenza A viruses.
According to the company, convenient Titration of EX-CELL Glycosylation Adjust (Gal+) into the bioreactor allows users to directionally adjust their product to match the specific reference profile.
Glycosylation of the HA gene, which is important for neutralization of the antigenic sites (25) and proper folding of the proteins, has big influence on the antigenicity and immunogenicity of the HA glycoprotein.
Interestingly, this protein was expressed in eukaryotic cell vectors, and a sequence analysis suggests that there may be several potential glycosylation sites.
Other topics include disulfide bond formation, lipid transport, n-linked protein glycosylation, insertion of tail-anchored membrane proteins, and how viruses use the endoplasmic reticulum for entry and replication.

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