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  2. Glycosyltransferase - Wikipedia

    en.wikipedia.org/wiki/Glycosyltransferase

    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 ...

  3. Trypsin - Wikipedia

    en.wikipedia.org/wiki/Trypsin

    Trypsin digestion of extra cellular matrix is a common practice in cell culture. However, this enzymatic degradation of the cells can negatively effect cell viability and surface markers, especially in stem cells. There are gentler alternatives than trypsin such as Accutase which doesn't effect surface markers such as cd14, cd117, cd49f, cd292.

  4. Protein catabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_catabolism

    Protein degradation differs from protein catabolism. Proteins are produced and destroyed routinely as part of the normal operations of the cell. Transcription factors, proteins that help regulate protein synthesis, are targets of such degradations. Their degradation is not a significant contributor to the energy needs of the cell. [3]

  5. Cell wall protein 2 - Wikipedia

    en.wikipedia.org/wiki/Cell_wall_protein_2

    Cell Wall Protein 2 (CWP2) is a cell mannoprotein that is covalently bonded to the cell wall and serves as a significant component of the cell wall structure. Generally, mannoproteins are special glycoproteins specifically in the outer part of the yeast cell wall and contributes to the yeast's ability to withstand acidic conditions in ...

  6. Peptidoglycan glycosyltransferase - Wikipedia

    en.wikipedia.org/wiki/Peptidoglycan_glycosyl...

    proteins Peptidoglycan glycosyltransferase ( EC 2.4.1.129 ) is an enzyme used in the biosynthesis of peptidoglycan . It transfers a disaccharide-peptide from a donor substrate to synthesize a glycan chain.

  7. Trypsin inhibitor - Wikipedia

    en.wikipedia.org/wiki/Trypsin_inhibitor

    A trypsin inhibitor (TI) is a protein and a type of serine protease inhibitor that reduces the biological activity of trypsin by controlling the activation and catalytic reactions of proteins. [1] Trypsin is an enzyme involved in the breakdown of many different proteins , primarily as part of digestion in humans and other animals such as ...

  8. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Protein anabolism is the process by which proteins are formed from amino acids. It relies on five processes: amino acid synthesis, transcription, translation, post translational modifications, and protein folding. Proteins are made from amino acids. In humans, some amino acids can be synthesized using already existing intermediates. These amino ...

  9. Cell wall - Wikipedia

    en.wikipedia.org/wiki/Cell_wall

    The cell wall might have evolved to deter viral infections. Proteins embedded in cell walls are variable, contained in tandem repeats subject to homologous recombination. [17] An alternative scenario is that fungi started with a chitin-based cell wall and later acquired the GT-48 enzymes for the 1,3-β-glucans via horizontal gene transfer. The ...