Chymotrypsin. therapeutic enzyme

A novel concept of using bioadhesive polymers as enzyme inhibitors has been developed [97]. Included are derivatives of poly acrylic acid, polycarbophil, and car-bomer to protect therapeutically important proteins and peptides from proteolytic activity of enzymes, endopeptidases (trypsin and a-chymotrypsin), exopeptidases (carboxypeptidases A and B), and microsomal and cytosolic leucine aminopeptidase. However, cysteine protease (pyroglutamyl aminopeptidase) is not inhibited by polycarbophil and carbomer [97]. 

Chymotrypsin [ban, inn] (EC 3.4.21.1 Catarase Zonulysin ) is an enzyme (MW c. 25,0(X) a-form). It is a (serine) endopeptidase stored as zymogen in granules of pancreatic P-cells of mammals. It catalyses the hydrolysis of amide and ester bonds of peptides and proteins, particularly those adjacent to the carbonyl group of hydrophobic L-amino acids. Therapeutically, it is used in ocular surgery, especially for removal of cataracts. It was used formerly as a... 

Chymotrypsin has been successfully immobilized by carbodi-imide-mediated reaction with heparin.Catalytic properties of the modified enzyme, which is of potential importance therapeutically, were unchanged while the enzyme s thermal stability was improved. 

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