Information om | Engelska ordet CHYMOTRYPSIN

Exempel på hur man kan använda CHYMOTRYPSIN i en mening

• Moreover, chymotrypsin induces its own activation by cleaving in positions 14–15, 146–147, and 148–149, producing α-chymotrypsin (which is more active and stable than π-chymotrypsin).
• Chymotrypsinogen is an inactive precursor (zymogen) of chymotrypsin, a digestive enzyme which breaks proteins down into smaller peptides.
• 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.
• Then the proteins are cut into several fragments using proteolytic enzymes such as trypsin, chymotrypsin or Glu-C.
• A serine in each of trypsin and chymotrypsin was identified as the catalytic nucleophile (by diisopropyl fluorophosphate modification) in the 1950s.
• 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.
• In 1962, Westheimer and others demonstrated the synthesis of p-nitrophenyl diazoacetate and the subsequent acylation of chymotrypsin to form diazoacetylchymotrypsin, which was then photolyzed.
• 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.
• For example, proteases such as chymotrypsin contain an oxyanion hole to stabilise the tetrahedral intermediate anion formed during proteolysis and protects substrate's negatively charged oxygen from water molecules.
• It is one of the three serine proteases of the chymotrypsin family that are stored in the azurophil granules, and also a member of the peptidase S1 protein family.
• In other words, the collagens can be subjected to a short digestion by proteinases called trypsin and chymotrypsin at increasing temperatures.
• Unlike many eukaryotic proteasomes, which have several different peptide substrate specificities, hslV has a specificity similar to that of chymotrypsin; hence it is inhibited by proteasome inhibitors that specifically target the chymotrypsin site in eukaryotic proteasomes.
• It inactivates many serine proteases, including trypsin, chymotrypsin, kallikrein, plasmin, granulocyte elastase, cathepsin, thrombin, and factors IXa, Xa, XIa, and XlIa.
• Like most of the human elastases, elastase 3B is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine.
• Heavy meromyosin (HMM) is the larger of the two fragments obtained from the muscle protein myosin II following limited proteolysis by trypsin or chymotrypsin.
• Like most of the human elastases, elastase 3A is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine.
• STI is a large (20,100 daltons), strong inhibitor of trypsin, while BBI is much smaller (8,000 daltons) and inhibits both trypsin and chymotrypsin.
• Structures have been determined for several members of the subtilisin family showing that subtilisins exploit the same catalytic triad as the chymotrypsins although the residues occur in a different order (His/Asp/Ser in chymotrypsin and Asp/His/Ser in subtilisin); otherwise the structures show similarity to no other proteins.
• Many CUB-containing proteins are peptidases belonging to MEROPS peptidase families M12A (astacin) and S1A (chymotrypsin).
• The early crystal structures included chymotrypsin (PDB file 2CHA), chymotrypsinogen (PDB file 1CHG), trypsin (PDB file 1PTN), and elastase (PDB file 1EST).

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