Chymotrypsin kallikrein plasmin

Aprotinin is a polypeptide consisting of a chain of 58 amino acid residues, which inhibits stoichiometrically the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin, and trypsin. Aprotinin is obtained from bovine tissues and purified by a suitable process. It is stored as a bulk solution or lyophilized powder. The amount of two related substances des-Ala-des-Gly-aprotinin and des-Ala-aprotinin is determined by CZE with a 100% analysis. The relative migration times are 0.98 for des-Ala-des-Gly-aprotinin and 0.99 for des-Ala-aprotinin, and the specified limits are 8.0 and 7.5%, respectively. 

Bik inhibits the trypsin serine proteases through binding of either of its two Kunitz domains. Depending on the serine protease and the Kunitz domain involved, dissociation constants (K ) range from 0.03 to 800 pM [6, 28]. Bik fragmentation and glycation also effect strength and specificity of inhibition. For example, trypsin, chymotrypsin, kallikrein, plasmin, elastase, and cathepsin are inhibited at a A) of 0.03-3 pM, whereas Factors IXa, Xa, XIa, and Xlla are less inhibited with a A) of 15-800 pM. Protease inhibition is observed with both Kunitz domains except for Factors IXa and Xa that... 

A polypeptide obtained from bovine tissues and consisting of a chain of 58 amino acids. It inhibits stoichiometrically the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin, and trypsin. 

Serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein, and plasmin Binding is reversible, with most aprotinin-protease complexes dissociating at pH>10or <3 Peptidase inhibitor... 

Aprotinin is a polypeptide consisting of 58 amino acid residues derived from bovine lung tissues and shows inhibitory activity toward various proteolytic enzymes including chymo-trypsin, kallikrein, plasmin, and trypsin. It was also one of the first enzyme inhibitors used as an auxiliary agent for oral (poly)peptide administration. The co-administration of aprotinin led to an increased bioavailability of peptide and protein drugs [5,44,45], The Bowman-Birk inhibitor (71 amino acids, 8 kDa) and the Kunitz trypsin inhibitor (184 amino acids, 21 kDa) belong to the soybean trypsin inhibitors. Both are known to inhibit trypsin, chymotrypsin, and elastase, whereas carboxypeptidase A and B cannot be inhibited [7,46],... 

Tobacco-produced recombinant research-grade bovine aprotinin (Apronexin NP) [238] is also available from Sigma Aldrich. Aprotinin is a protease inhibitor which is used as a research reagent in biomanufacturing for several therapeutic applications. It has been traditionally extracted from bovine lung tissue. Aprotinin is a single, 58 amino-acid polypeptide with three disulfide bonds, and inhibits several serine proteases such as trypsin, chymotrypsin, plasmin, and kallikrein. 

The pancreatic trypsin inhibitor binds to trypsin, chymotrypsin, plasmin, and kallikrein, but does not inhibit elastase and subtilisin. Model-building studies of the inhibitor chymotrypsin complex show that the enzyme and Inhibitor have highly complementary structures. If Lys-15 (in a non-protonated form) is placed in the spedficity pocket with the C and NH of Lys-15 in similar positions to those of tryptophan in the formyl-L-tryptophan-chymotrypsin complex, the residues on the AT-terminal side of lysine then form an antiparallel jS-structure with the enzyme similar to that proposed for y-chymostrypsin (1). There appear to be a number of favourable hydro-... 

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