Information om | Engelska ordet TRYPSIN

Exempel på hur man kan använda TRYPSIN i en mening

• Trypsin activates chymotrypsinogen by cleaving peptidic bonds in positions Arg15 – Ile16 and produces π-chymotrypsin.
• Tryptophan is named after the digestive enzymes trypsin, which were used in its first isolation from casein proteins.
• Amylase/trypsin inhibitor, a substance that inhibits the enzymes amylase or trypsin (see Non-celiac gluten sensitivity).
• It is one of three principal endopeptidases (enzymes cutting proteins in the middle) in the human digestive system, the other two being chymotrypsin and trypsin.
• It is cleaved to its active form, trypsin, by enteropeptidase, which is found in the intestinal mucosa.
• TPCK-treated trypsin is used to improve infection yield in laboratory tissue culture of some wild virus isolates that are not well-adapted to growth in vitro, such as some low-pathogenic avian influenza strains or fresh clinical isolates of SARS-CoV-2.
• The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.
• By ensiling the fruits, drying and heat treatment to deactivate the trypsin inhibitor can be avoided.
• Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin.
• As part of the parasite defense strategy, Ascaris roundworms secrete a series of inhibitors to target digestive and immune-related host proteases, which include pepsin, trypsin, chymotrypsin/elastase, cathepsins, and metallocarboxypeptidases (MCPs).
• Then the proteins are cut into several fragments using proteolytic enzymes such as trypsin, chymotrypsin or Glu-C.
• Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes.
• For subculture, cells may be detached by one of several methods including trypsin treatment to break down the proteins responsible for surface adherence, chelating calcium ions with EDTA which disrupts some protein adherence mechanisms, or mechanical methods like repeated washing or use of a cell scraper.
• A serine in each of trypsin and chymotrypsin was identified as the catalytic nucleophile (by diisopropyl fluorophosphate modification) in the 1950s.
• Of these compounds, atranorin showed the highest inhibition of proteolytic enzymes trypsin and porcine pancreatic elastase.
• Okara contains some antinutritional factors: trypsin inhibitors (mostly destroyed by cooking), saponins, and soybean agglutinins, which cannot be easily digested.
• It is formed in the pancreas and activated to trypsin with enteropeptidase Chymotrypsinogen is the inactive form of chymotrypsin and has similar functions as trypsin.
• Aprotinin is a competitive inhibitor of several serine proteases, specifically trypsin, chymotrypsin and plasmin at a concentration of about 125,000 IU/ml, and kallikrein at 300,000 IU/ml.
• Immunohistochemical analyses indicate that the cells in NF usually express smooth muscle actin, muscle specific actin, and vimentin proteins but generally do not express CD34, S-100 protein, desmin, trypsin, factor VIII, F4/80, or HLA-DR1 proteins.
• In the case of pancreatic carboxypeptidase A, the inactive zymogen form - pro-carboxypeptidase A - is converted to its active form - carboxypeptidase A - by the enzyme trypsin.

Förberedelsen av sidan tog: 370,78 ms.