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  1. Nine transglutaminases have been characterised in humans, [5] eight of which catalyse transamidation reactions. These TGases have a three or four-domain organization, with immunoglobulin -like domains surrounding the central catalytic domain.

  2. 25 wrz 2021 · Microbial transglutaminase and its complexes increase intestinal permeability, suppresses enteric protective pathways, enhances microbial growth and gliadin peptide’s epithelial uptake and can transcytose intra-enterocytically to face the sub-epithelial immune cells.

  3. 2 sty 2020 · Transglutaminase (EC 2.3.2.13, protein-glutamine gamma-glutamyltransferase, TGase) is a calcium-dependent enzyme, belonging to the class of transferases, which catalyzes the acyl-transfer between glutamine residues and a wide variety of primary amines (Ohtsuka et al. 2000).

  4. 25 cze 2014 · Our group has identified a transglutaminase in the oomycete Phytophthora cinnamomi, which is able to induct defense responses and disease-like symptoms. In this mini-review, we report the achievements in this area in order to illustrate the importance and the versatility of transglutaminases.

  5. 22 paź 2013 · Transglutaminases (TGases) are a family of enzymes (EC 2.3.2.13) that catalyze an acyl-transfer reaction between the γ-carboxamide group of a protein- or peptide-bound glutamine and the ε-amino group of a lysine residue, resulting in the formation of a relatively protease-resistant isopeptide bond [2] (Figure 1).

  6. 26 gru 2019 · Instead, the use of transglutaminase for the covalent attachment of PEG molecules to pharmaceutical proteins shows stringent substrate specificity, and site specific modification or PEGylation of the Gln residues bound to the proteins on the substrates can be obtained.

  7. 1 lut 2003 · Transglutaminases (TGs) are Ca 2+ -dependent enzymes that post-translationally modify specific glutaminyl (Gln) side-chains in proteins by deamidation, transamidation or esterification.

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