EC Number   |
Application |
Reference |
|---|
   3.4.21.4 | analysis |
application of biotinylated trypsin as a sensitive versatile probe for the detection and characterization of an ovine chondrocyte serine proteinase inhibitor using Western blotting |
95456 |
| 3.4.21.4 | analysis |
comparison of five crystals of bovine trypsin obtained under analogous conditions. The Calpha and backbone atoms of the structures superpose very well. The occupancy of ligands in regions of low thermal motion is reproducible, whereas solvent molecules containing heavier atoms (such as sulfur) or those located on the surface can differ significantly. The coordination lengths of the calcium ion are conserved. A large proportion of the multiple conformations refine to similar occupancies and the residues adopt similar orientations. The protonation states of histidine residues and carboxylate moieties is consistent for all of the models. However, several features of residues or ligands located in flexible parts of the macromolecule may vary significantly, such as side-chain orientations and the occupancies of certain fragments |
731053 |
| 3.4.21.4 | analysis |
detection of enzyme hydrolytic activity by use of 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate coupled to a chymotryptic petide obtained from hemoglobin on silica gel plate. Detection of 45 fmol of enzyme at 25°C within 1 min |
668005 |
| 3.4.21.4 | analysis |
experimental system for the structural and physico-chemical analysis of factor Xa inhibitors in trypsin variants with factor Xa phenotype: E97N/Y99L, S190A, E97N/Y99L/S190A |
650468 |
| 3.4.21.4 | analysis |
the double mutant trypsinogen D189S/DELTA223 lacks trypsin-like activity but aquires a rather unique selectivity, it preferentially hydrolyses peptide bonds C-terminal to tyrosyl residues. This narrow specificity should be useful in peptide-analytical applications such as sequence-specific fragmentation of large proteins prior to sequencing |
649322 |
| 3.4.21.4 | biotechnology |
enzyme molecules are associated with the outer protein layer of rotavirus virions propagated in cell culture medium containing the enzyme. Enzyme is present only in triple-layer particles, not in double-layer particles. Enzyme associated with virions is inactive, activity is recovered only when the outer capsid is solubilized. Incorporation of trypsin into rotavirus particles may enhance its infectivity |
669689 |
| 3.4.21.4 | biotechnology |
recombinant Streptomyces erythraeus trypsin is fundamental to the use for proteomics applications |
699820 |
| 3.4.21.4 | food industry |
the enzyme can be used as a possible biotechnological tool in the fish processing and food industries |
708530 |
| 3.4.21.4 | medicine |
commercial-level production of trypsin in transgenic maize, the availability of this reagent should allow for the replacement of animal-derived trypsin in the processing of pharmaceutical proteins |
650668 |
| 3.4.21.4 | medicine |
dental plaque is a causative factor for oral disease and a potential reservoir for respiratory infection in the elderly. Therefore, there is a critical need for the development of effective methods to remove oral biofilm. Proteases reduce oral biofilm in vivo in elderly subjects. Tablets containing actinidin remove tongue coating in elderly subjects. Oral Actinomyces biofilm is significantly reduced by the proteases papain, actinidin and trypsin. Papain and trypsin effectively digest the major fimbrial proteins, FimP and FimA, from Actinomyces. Actinidin, papain and trypsin reduce multispecies biofilm that is reconstructed in vitro. Papain and trypsin inhibit formation of multispecies biofilm in vitro |
752608 |
