Biomaterial Database

Alkyl isocyanates as active site-specific inhibitors of chymotrypsin and elastase. 1971

W E Brown, and F Wold

Alkyl isocyanates react specifically with the two serine proteinases, chymotrypsin and elastase, to yield inactive enzyme derivatives containing 1 male of reagent per mole of enzyme. Octyl isocyanate inactivates chymotrypsin only, while butyl isocyanate inactivates both enzymes but shows greater efficiency toward elastase than toward chymotrypsin. These reagents may thus represent unique chemical "yardsticks" for the measurement of the relative dimensions of the active sites of the two very similar enzymes.

UI	MeSH Term	Description	Entries
D010196	Pancreatic Elastase	A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.	Elastase,Pancreatopeptidase,Elastase I,Pancreatic Elastase I,Elastase I, Pancreatic,Elastase, Pancreatic
D002918	Chymotrypsin	A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.	Alpha-Chymotrypsin Choay,Alphacutanée,Avazyme
D003485	Cyanates	Organic salts of cyanic acid containing the -OCN radical.	Cyanate
D000478	Alkylation	The covalent bonding of an alkyl group to an organic compound. It can occur by a simple addition reaction or by substitution of another functional group.	Alkylations
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining