Chymotrypsin

The disease is a proteolytic enzyme pancreatic juice. The disease is secreted in an inactive state - in the form of chymotrypsinogen, turns into a disease under the action of the enzyme trypsin (see).
Optimum action of chymotrypsin at pH =7,6-8,2. Like trypsin disease hydrolyzes proteins and gelatin with the formation of low-molecular peptides (see), but the enzyme largely those of the peptide bond, which trypsin is not valid. Digestive ability fecal sometimes used to cleanse the wound surfaces, and also for the dissolution of blood clots.

Himotripsina group of proteolytic enzymes in the pancreatic juice. Himotripsina are produced in acinar cells of the pancreas in the form of inactive precursors - chymotrypsinogen into himotripsina under the effect of trypsin (see). During the activation process the most well studied chymotrypsinogen And(a) the formation of a number of himotripsina (p, Delta that alpha, beta, V), which has very similar properties. Most Agricultural received in crystalline form. The most common is α Agricultural; mol. the weight is 25 000, isoelectric point at pH of 8.6. Molecule α Agricultural consists of 3 polypeptide chains, the United disulfide bonds, and contains approximately 240 amino acid residues; the chemical structure of this disease completely deciphered. It is stable at pH 3, pH = 1 & rn = 10 irreversibly inactivated; at pH 6-9 observed autolysis (self-digestion).
Z - component of the enzymes in the active center of which are the remains of histidine and serine. The Agricultural activity is oppressed by diisopropyldithiophosphate and related compounds.
Himotripsina hydrolyzing proteins, peptides and synthetic substrates: amides and esters. Mainly split connections obtained amino acid residues with hydrophobic side chains. Optimum action of Agriculture - at pH = 7,6-8,2; at pH 5-6 they have the ability to storativity milk.
X. sometimes used in the treatment of wounds and thrombosis. Cm. also Enzymes.