The inactivation of streptomyces-derived proteinase inhibitors by mammalian tissue preparations.
The proteinase inhibitors leupeptin and chymostatin are inactivated by preparations of perfused mouse liver. The inhibitors are degraded maximally at neutral or alkaline pH values. The inactivating enzymes are inhibited by Dip-F and pms-F but not by EDTA, 1,10 phenanthroline or iodoacetic acid. The significance of these results is discussed in terms of the potential of the inhibitors as antiproteolytic drugs.
D000818:Animals; D010450:Endopeptidases / Q000494:pharmacology; D005260:Female; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007976:Leupeptins / Q000037:antagonists & inhibitors*; D008099:Liver / Q000201:enzymology*; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D009842:Oligopeptides / Q000037:antagonists & inhibitors*; D011480:Protease Inhibitors; D012697:Serine Endopeptidases
D007976:Leupeptins; D009842:Oligopeptides; D011480:Protease Inhibitors; C002101:chymostatin; D010450:Endopeptidases; D012697:Serine Endopeptidases