Interactions in vitro and in vivo between anionic and cationic porcine trypsin and porcine plasma proteinase inhibitors.
A method for purifying porcine anionic and cationic trypsin is presented. Reaction mixtures with increasing amounts of the two porcine trypsins and porcine serum were studied in vitro to evaluate the relative importance of alpha 1-macroglobulin and alpha 2-macroglobulin as well as alpha 1-proteinase inhibitor in the rapid binding of porcine anionic and cationic trypsin. Porcine cationic trypsin was preferentially bound to alpha 1-macroglobulin, while anionic trypsin exhibited equal binding to both alpha-macroglobulins. Both trypsins were also bound by the alpha 1-proteinase inhibitor but not until alpha 1-macroglobulin approached saturation. Trypsin-alpha-macroglobulin complexes were cleared from plasma with a half-life of 6 min. For trypsin-alpha 1-proteinase inhibitor-complexes the half-life was 120 min. These findings are in accordance with results for other mammalian species, including man.
Hjelmqvist
B
B
Institutionen för kirurgisk patofysiologi, Lunds Universitet, Malmö Allmänna Sjukhus, Sweden.
Borgström
A
A
Ohlsson
K
K
D000818:Animals; D002850:Chromatography, Gel; D004587:Electrophoresis, Agar Gel; D007123:Immunoelectrophoresis, Two-Dimensional; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D010189:Pancreatic Juice / Q000201:enzymology; D011480:Protease Inhibitors / Q000097:blood*; D013552:Swine; D014357:Trypsin / Q000302:isolation & purification / Q000378:metabolism*
D007527:Isoenzymes; D011480:Protease Inhibitors; D014357:Trypsin