deamidation


Also found in: Medical, Wikipedia.

deamidation

[dē‚am·ə′dā·shən]
(organic chemistry)
Removal of the amido group from a molecule.
References in periodicals archive ?
Tau is also extensively modified posttranslationally and has been reported to be modified by phosphorylation, acetylation, glycosylation, glycation, deamidation, isomerization, nitration, methylation, ubiquitylation, sumoylation, and truncation.
Most polypeptide drugs are sensitive to pH variety in GIT, and pH variation results in pH-induced oxidation, deamidation, and hydrolysis reactions which constitute chemical barriers to absorption (15).
In addition, Catalent Biologics analytical services will be showcasing expert posters on The Use of LC-MS to Monitor Levels of Oxidation and Deamidation in Proteins for Release and Stability by Anne Marie Rogan, Senior Associate Scientist and Quantitation and Characterization of Polysorbate-80 by HPLC and Charged Aerosol Detection by Luke Deters, Senior Manager, Large Molecule Analytical Chemistry.
da Fonseca-Wollheim F, Deamidation of glutamine by increased plasma gamma-glutamyltransferase is a source of rapid ammonia formation in blood and plasma specimens.
It is also utilized in facilitating some chemical reaction like deamidation, rearrangement, cyclization and imidation [17].
A stress protein on their surface is presented, permeability changes results in the entry of gliadin in laminapropria, where its deamidation by an enzyme tissue transglutaminase, allowing its interaction with HLA-DQ2 (or HLA-DQ8) on antigen presenting cell's surface.
Tissue transglutaminase plays an important role as it crosslinks gliadin and cause its deamidation into glutamic acid and gliadin peptide.
Deamidation of collagen makes it a useful and important biopolymer in the field of bio-material engineering.
Less critical were truncated variants, norleucine and deamidation, all of which were assessed using some form of chromatography.
The unique growth pattern of the human lens and accrual of new lens fibers onto existing cell layers coupled with no protein turnover and an age-related depletion of [alpha]-crystallin chaperone function render the human lens vulnerable to posttranslational modifications such as phosphorylation, glycation, deamidation, and aggregation which are caused by oxidative stress and decline of antioxidant enzymes [7-9].
Deamidation of asparagine and glutamine and oxidation of methionine were selected for the search parameters as variable modification, and carbamidomethyl modification of cysteine was used as a fixed modification.
Deamidation is considered as the most common route for chemical degradation of proteins, peptides and antibodies (15,16).