A drug-carrier matrix has been developed which protects embedded insulin from degradation by the luminally secreted serine-proteases trypsin (EC 3.4.21.4), chymotrypsin (EC 3.4.21.1) and elastase (EC 3.4.21.36) in vitro. Increasing amounts of the Bowman-Birk inhibitor (BBI) and elastatinal, respectively, were
The inhibitory power of three different active Nylon membranes, separately loaded with three different protease inhibitors, was studied with the aim of reducing the increased elastase concentration occurring during hemodialysis or extracorporeal blood circulation in patients undergoing cardiopulmonary bypass. Chemical
Effects of elastatinal, a protease inhibitor, on DNA repair and its cytotoxicity were investigated in normal human, xeroderma pigmentosum and Chinese hamster V79 cells. There were no effects of elastatinal on DNA repair and UV-induced sister chromatid exchanges, and all
Microbial protease inhibitors elastatinal and leupeptin were tested for cytotoxicity and for effects on spontaneous and u.v.-induced 6-thioguanine-resistant (6TGr) mutation and sister-chromatid exchange (SCE) in V79 Chinese hamster cells. Continuous treatment with elastatinal exhibited marked cytotoxicity, while leupeptin was almost
Human leukocyte elastase can be proteolytically inactivated by bovine pancreatic trypsin. Neither porcine pancreatic elastase nor bovine pancreatic chymotrypsin causes inactivation of leukocyte elastase, nor are trypsin, pancreatic elastase, or chymotrypsin themselves susceptible to proteolysis. The trypsin-catalyzed inactivation of leukocyte
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