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	Biol. Chem. Hoppe-Seyler Apr (1988); 369(4):309-15
Interactions in vitro and in vivo between human and porcine cationic pancreatic elastase and plasma protease inhibitors.
Hakansson HO, Ohlsson K
Department of Surgery, University of Lund, Malmo General Hospital, Sweden.
Abstract: Trace amounts of porcine pancreatic elastase mixed with porcine serum, or injected intravenously into the pig, were found to be bound mainly to alpha 1- and alpha 2-macroglobulin (90%). Alpha 1-macroglobulin approached saturation with elastase before significant binding to alpha 2-macroglobulin was demonstrable. Human pancreatic cationic elastase showed in human serum preferential binding to alpha 2-macroglobulin, but the elastase was also bound by alpha 1-protease inhibitor and by alpha 1-antichymotrypsin. The porcine elastase-alpha 1 alpha 2-macroglobulin complexes injected intravenously or formed in vivo in the pig were rapidly eliminated from the blood stream following a first order reaction with t 1/2 = 8 min. Porcine alpha 1-protease-inhibitor-bound elastase disappeared considerably more slowly.
[PUBMED: 2456771]