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The associated anti-A and anti-B antibodies are usually IgM antibodies, produced in the first years of life by sensitization to environmental substances such as food, bacteria, and viruses. The ABO blood types were discovered by Karl Landsteiner in 1901; he received the Nobel Prize in Physiology or Medicine in 1930 for this discovery. [ 5 ]
80908 Ensembl ENSG00000175164 ENSG00000281879 ENSMUSG00000015787 UniProt P16442 P38649 RefSeq (mRNA) NM_020469 NM_030718 NM_001290444 RefSeq (protein) NP_065202 NP_001277373 NP_109643 Location (UCSC) Chr 9: 133.23 – 133.28 Mb Chr 2: 26.73 – 26.75 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Histo-blood group ABO system transferase is an enzyme with glycosyltransferase activity ...
Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...
If the person is a secretor, the antibodies will bind to the antigens in their saliva rather than the red blood cells, and will not cause red blood cells to agglutinate. [5]: 25 Secretor status testing was historically used in forensic science, but this has been made obsolete by advances in DNA testing. [6]: 226
Glycosylation is an important parameter in the optimization of many glycoprotein-based drugs such as monoclonal antibodies. [6] Glycosylation also underpins the ABO blood group system. It is the presence or absence of glycosyltransferases which dictates which blood group antigens are
OGT cleaves Host Cell Factor C1, at one or more of 6 repeating 26 amino acid sequences. The TPR domain of OGT binds to the carboxyl terminal portion of an HCF1 proteolytic repeat so that the cleavage region is in the glycosyltransferase active site above uridine-diphosphate-GlcNAc [11] The large proportion of OGT complexed with HCF1 is necessary for HCF1 cleavage, and HCFC1 is required for OGT ...
UGGT, or UDP-glucose:glycoprotein glucosyltransferase, is a soluble enzyme resident in the lumen of the endoplasmic reticulum (ER). [1]The main function of UGGT is to recognize misfolded glycoproteins and transfer a glucose (Glc) monomer (monoglucosylate) to the terminal mannose of the A-branch of the glycan on the glycoprotein.
The heavy glycosylation of these proteins can mask peptide epitopes, making designing antibodies targeted to certain proteins sections all the more difficult. Therefore, some have turned to translational glycobiology to develop antibodies using semi-synthetic and fully synthetic oligosaccharides as antigens.
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