Proteinase Inhibitors of Microbial Origin A Review

Property of kinin-forming enzyme in rat stomach.

“…TLCK has been shown to be a specific inhibitor of trypsin (12). Pepstatin A shows no inhibition against kallikrein, plasmin, trypsin, papain, chymotrypsin, thrombokinase and thrombin, but is a specific inhibitor of acid proteases, cathepsin D and pepsin (11). Chymostatin is an inhibitor towards papain, chymotrypsin, cathepsin A, B and D, but it has no appreciable effect on pepsin (11).…”

“…Trasylol inhibits plasma, salivary and urinary kallikreins, plasmin, trypsin, papain and chy motrypsin, but does not inhibit rat pancreatic kallikrein (3,11). SBTI inhibits plasma kallikrein, trypsin and chymotrypsin (3,11).…”

“…SBTI inhibits plasma kallikrein, trypsin and chymotrypsin (3,11). TLCK has been shown to be a specific inhibitor of trypsin (12).…”

Pharmacological activities of a kinin released from rat plasma by catheptic enzyme in rat stomach.

“…The catheptic enzymes of polymorphonuclear leukocytes (PMN cells) and macrophages release leukokinins at around pH 5.0, and their enzyme activities are inhibited by pepstatin, but not by trasylol (11). Cathepsin D is inhibited by not only pepstatin but also by chymostatin (12). Pepsin released MLBK from the plasma protein at pH 1.0 (13), and its enzyme activity is inhibited by pepstatin, but not by chymostatin (12).…”

“…Cathepsin D is inhibited by not only pepstatin but also by chymostatin (12). Pepsin released MLBK from the plasma protein at pH 1.0 (13), and its enzyme activity is inhibited by pepstatin, but not by chymostatin (12). The KFE was characteris tically similar to cathepsin D with respect to its specific inhibitors and the optimum pH, which was distinct from gastrointestinal kallikrein and pepsin (2).…”