Tissue and subcellular distribution of enzymes inactivating leupeptin.
Leupeptin, a proteinase inhibitor obtained from culture filtrates of Streptomyces sp., has been proposed as a valuable agent for the restriction of proteolysis in vivo. We have previously shown that mammalian tissues possess an enzymic system that is capable of inactivating leupeptin (Beynon RJ, Brown CP & Butler PE, 1981, Acta Biol. Med. Germ. 40, 1539-1546). This paper demonstrates the ubiquitous distribution of the inactivating system throughout mammalian tissues and provides evidence for the location of the enzyme(s) in the soluble fraction of the cell.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D010450:Endopeptidases / Q000032:analysis*; D005260:Female; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007413:Intestinal Mucosa / Q000201:enzymology; D007976:Leupeptins / Q000037:antagonists & inhibitors; D008099:Liver / Q000201:enzymology; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D009130:Muscle, Smooth / Q000201:enzymology; D012697:Serine Endopeptidases; D013347:Subcellular Fractions / Q000201:enzymology*
D007976:Leupeptins; D010450:Endopeptidases; D012697:Serine Endopeptidases; C037964:leupeptinase