title: Elastase inhibitor from mammalian neutrophil cytosol.
abstract: Bovine, pig and horse leukocyte elastase inhibitors represent the first example of functionally active intracellular serpin. Sequence analysis yields data indicating that the reactive site encompasses P1-P'1 Ala-Met sequence. Oxidation of swine (as well as equine) inhibitor reduced its association rate constants kon with the tested enzymes (by at least 1 order of magnitude). However in case of bovine inhibitor, only a slight reduction has been observed for human neutrophil elastase but not for chymotrypsin or pancreatic elastase.
authors.affiliation: Institute of Molecular Biology, Jagiellonian University, Kraków, Poland.
authors.forename: E
authors.initials: E
authors.lastname: Korzus
authors.forename: A
authors.initials: A
authors.lastname: Dubin
authors.forename: J
authors.initials: J
authors.lastname: Potempa
authors.forename: J
authors.initials: J
authors.lastname: Travis
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003600:Cytosol / Q000378:metabolism; D006736:Horses; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000378:metabolism*; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D015842:Serine Proteinase Inhibitors / Q000097:blood* / Q000737:chemistry; D015843:Serpins; D013552:Swine
chemical_list: D015842:Serine Proteinase Inhibitors; D015843:Serpins; D010196:Pancreatic Elastase