• peptides
  • Chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly those containing leucine and methionine at the P1 position. (wikipedia.org)
  • substrate
  • The reaction of chymotrypsin with its substrate was found to take place in two stages, an initial "burst" phase at the beginning of the reaction and a steady-state phase following Michaelis-Menten kinetics. (wikipedia.org)

Warning: preg_replace(): Compilation failed: unmatched parentheses at offset 8 in /home/lookformedical/www/faq.php on line 152
  • Specificity
  • The phenylalanine moiety is bound to the enzyme because of specificity for aromatic amino acid residues at the active site (as in chymotrypsin, in which it binds to the Histidine-57 residue in the active site). (wikipedia.org)
  • structure
  • The structure of chymotrypsin was solved by X-ray crystallography in the 1960s, showing the orientation of the catalytic triad in the active site. (wikipedia.org)
  • activity
  • The rennet activity of chymo-trypsin (or pepsin) is conveniently measured by allowing a standard solution of milk to which chymotrypsin has been added to flow slowly through a graduated pipette and observing the rate and distance of flow of the milk before it clots. (rupress.org)