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Chymotrypsin

Chymotrypsin is a proteolytic enzyme of pancreatic juice. Chymotrypsin is produced in an inactive state - as a chymotrypsinogen, which turns into chymotrypsin under the action of the enzyme trypsin (see).

The optimum action of chymotrypsin at pH = 7.6-8.2. Like trypsin, chymotrypsin hydrolyzes proteins and peptones to form low-molecular peptides (see), but breaks down mainly those peptide bonds to which trypsin does not act. The digestive ability of chymotrypsin is sometimes used to cleanse wound surfaces, as well as to dissolve blood clots.

Chymotrypsins are a group of proteolytic enzymes contained in pancreatic juice. Chymotrypsins are produced in the acinar cells of the pancreas as inactive precursors - chymotrypsinogens, which are converted to chymotrypsins by the action of trypsin (see). In the process of activation of the most well-studied chymotrypsinogen A (α), a series of chymotrypsins (n, δ, α, β, ү) are formed, which have very similar properties. Most chymotrypsins are obtained in crystalline form. The most common is α-chymotrypsin; they say its weight is 25,000, the isoelectric point is at pH = 8.6. The α-chymotrypsin molecule consists of 3 polypeptide chains connected by disulfide bonds, and contains about 240 amino acid residues; The chemical structure of this chymotrypsin is completely decoded. It is stable at a pH of about 3, at pH = 1 and pH = 10 is irreversibly inactivated; at pH = 6–9, autolysis (self-digestion) is observed.

Chymotrypsins are single-component enzymes whose active center contains histidine and serine residues. The activity of chymotrypsins is inhibited by diisopropylfluorophosphate and its related compounds.

Chymotrypsins hydrolyze proteins, peptides and synthetic substrates: amides and ethers. Preferably, the bonds formed by amino acid residues with hydrophobic side chains are cleaved. The optimum action of chymotrypsins - at pH = 7.6-8.2; at pH = 5-6, they have the ability to curdle milk.

Chymotrypsins are sometimes used in the treatment of wounds and thrombosis. See also Enzymes.