Isolation and characterization of rabbit plasma alpha-1-antiproteinase E.
Alpha-1-antiproteinase E, the fourth isoform of rabbit alpha-1-antiproteinase (alpha-1-antitrypsin) having a glutamic acid at the reactive center, has been purified from the plasma by sequential chromatography on hydroxyapatite and anion-exchange columns. The E form of alpha-1-antiproteinase formed a complex with trypsin, chymotrypsin, elastase, plasmin and pancreatic kallikrein as judged by SDS-PAGE. The E form inhibited elastase in a stoichiometric manner and chymotrypsin moderately, but the inhibition of trypsin was gradual. The F form inhibited trypsin most effectively followed by chymotrypsin and elastase. N-chlorosuccinimide reduced the elastase inhibitory activity of the E form, while the F form was more effectively inactivated by the oxidant.
Saito
A
A
Department of Biochemistry, School of Medicine, Kinki University, Osaka-Sayama, Osaka, Japan.
Sinohara
H
H
D000818:Animals; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D007536:Isomerism; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D011817:Rabbits; D013388:Succinimides / Q000494:pharmacology; D014357:Trypsin / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000097:blood / Q000302:isolation & purification; D000515:alpha 1-Antitrypsin / Q000302:isolation & purification* / Q000378:metabolism
D013388:Succinimides; D014361:Trypsin Inhibitors; D000515:alpha 1-Antitrypsin; C015752:N-chlorosuccinimide; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D014357:Trypsin