KLK11

(redirected from Trypsin-like protease)

KLK11

A gene on chromosome 19q13.33 that encodes a possible multifunctional serine protease which is expressed in the brain, skin and prostate.
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According to our data the wastes of sera production are a promising initial biomaterial for trypsin-like protease inhibitor obtain with antiviral properties and lower allergenicity.
The highest content of trypsin-like protease inhibitor was recorded in the fraction of the 5th isoform, which was the latter eluted from the column 0.
Proteolytic activation of seasonal human IAV HA occurs extracellularly or on the cell membrane in the airway by trypsin-type proteases, such as tryptase Clara, (19) mini-plasmin, (7) trypsin, (3) ectopic pancreatic trypsin, (4),(8),(10),(11),(21) porcine lung tryp tase, (22) TC30 (23) and type-II membrane bound proteases, human airway trypsin-like protease (HAT), transmembrane serine protease (TMPRSS)2 (24) and TMPRSS4 (25) (Table 1).
The more inhibited activity was the trypsin-like protease activity in the three species, with around 17% of inhibition in M.
Matriptase (also known as MT-SP1, ST14, TADG-15 and epithin) is a trypsin-like protease from the family of type II transmembrane serine proteases.
gemmatalis cuticle did not have a positive effect on trypsin-like protease (Pr2), since it was produced in substantive amounts in defined growth substrate (nitrate medium).
This shedding may be caused by trypsin-like protease activity, and the presence of such factors in BT products suggests a carryover of fermentation products as noted for [Beta]-lactamase (5,13).
The action of inhibitor of trypsin-like protease on influenza infection at the conditions of experiment", Infect Dis.
Trypsin-like proteases recognize highly basic residues in a substrate, and these enzymes are critical to Bt protoxin activation to enable midgut binding.
Entomopathogenic fungi produce distinct extracellular serine proteases, such as subtilisin-like proteases, trypsin-like proteases, metalloproteases, as well as several families of exo- acting peptidases that are believed to be important for host cuticle degradation (St.
The high content in basic residues of AMPs favors degradation by the trypsin-like proteases (Andreu & Rivas 1998), as observed in our experiments.