ABSTRACT The present study was carried out to investigate the effect of benazepril on corneal permeation in goat cornea and its effect on experimentally induced acute and chronic glaucoma in rabbits. Acute glaucoma was produced by i.v. infusion of 5% glucose (15ml / Kg) in rabbits, whereas chronic glaucoma was induced by injection of alpha-chymotrypsin into posterior chamber of rabbit eye. We s...

We recently described a monoclonal antibody, 10E5 , that completely blocks adenosine diphosphate (ADP) induced fibrinogen binding to platelets and aggregation induced by ADP, epinephrine, and thrombin. Multiple lines of evidence indicate that 10E5 binds to platelet membrane glycoproteins IIb and/or IIIa. Because it has been reported that platelets treated with chymotrypsin aggregate when fibrin...

Bowman-Birk inhibitors (BBIs) are cysteine-rich and highly cross-linked small proteins that function as specific pseudosubstrates for digestive proteinases. They typically display a "double-headed" structure containing an independent proteinase-binding loop that can bind and inhibit trypsin, chymotrypsin and elastase. In the present study, we used computational biology to study the structural c...

A procedure is described for the purification of the elastase and chymotrypsin-like enzymes from purulent sputum. This procedure permitted the isolation of 132 mg and 120 mg of the elastase and chymotrypsin-like enzymes, respectively, from 230 g of purulent sputum. The elastase enzymes consist of a family of five isozymes, and at least three isozymes comprise the chymotrypsin-like enzyme system...

The legume-derived Bowman-Birk trypsin and chymotrypsin protease inhibitors (BBI) are effective anticarcinogens in vivo and in vitro. The chymotrypsin-inhibitory domain has been shown to be responsible for this anticarcinogenic action. In this study we identify hydrolytic enzymes by their ability to hydrolyze the relatively specific chymotrypsin substrate succinyl-Ala-Ala-Pro-Phe-aminomethyl co...

The preparation of a new stable and active form of chymotrypsin is described. The enzyme possesses threonine-147 instead of alanineas the NH&erminal group of the C chain and has been called ai-chymotrypsin. The conformational transition that affects chymotrypsins at alkaline pH was investigated and compared with that of 01and &chymotrypsins by studying the kinetic constants and their pH depende...

Human digestive carboxypeptidases CPA1, CPA2, and CPB1 are secreted by the pancreas as inactive proenzymes containing a 94-96-amino acid-long propeptide. Activation of procarboxypeptidases is initiated by proteolytic cleavage at the C-terminal end of the propeptide by trypsin. Here, we demonstrate that subsequent cleavage of the propeptide by chymotrypsin C (CTRC) induces a nearly 10-fold incre...

Brown, Shupe, and Laskowski (1) have described the isolation, from beef pancreas, of a crystalline proteolytic enzyme which they have named “activated protein B” or “chymotrypsin B.” Through the kindness of Dr. Laskowski who provided us with a 4 times recrystallized sample of this enzyme, it was possible to examine its action on a series of synthetic peptides and peptide derivatives. The data p...

Serum protease inhibitor activity was assessed from the ability of the serum to inhibit casein hydrolysis by ct-chymotrypsin (EC 3.4.4.5). Unmodified AutoAnalyzer equipment was used in conjunction with a fluorimetric method for dialyzable tyrosyl peptides. Serum, diluted with tris(hydroxymethyl) aminomethane buffer, was added to a chymotrypsin solution to inhibit its activity. For 72 sera, the ...

Basic pancreatic trypsin inhibitor with disulfide bond 14-38 reduced by borohydride was reacted with sulfhydryl group reagents. The reduced inhibitor and the dithiobis (Z-nitrobenzoic acid) derivatives retained inhibitory activity toward both trypsin and cr-chymotrypsin. The carboxamidomethyl and aminoethyl derivatives were active toward trypsin but inactive with cu-chymotrypsin. The p-mercurib...