Differences between the binding of trypsin and chymotrypsin by alpha 1-proteinase inhibitor.
Complexes of alpha 1-proteinase inhibitor with proteases were examined by SDS-PAGE in 7.5% polyacrylamide gel and in a gel gradient. While the inhibitor-chymotrypsin complex was stable under both sets of conditions, the inhibitor-trypsin complex quantitatively dissociated under the second set of conditions, indicating that trypsin, unlike chymotrypsin, is not linked covalently to the inhibitor. Although the inhibitor sustained at least two discrete cleavages by trypsin, its overall recovery after dissociation was 100%. Due to an increased rate of autolytic breakdown in the presence of the inhibitor, the recovery of trypsin after dissociation was appreciably less than 100%. Based on these observations, a new theory of trypsin inhibition by alpha 1-proteinase inhibitor is proposed. This method is suitable for the examination of other inhibition systems as well.
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D002417:Cattle; D002918:Chymotrypsin / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D011480:Protease Inhibitors / Q000378:metabolism*; D011485:Protein Binding; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000378:metabolism*; D000515:alpha 1-Antitrypsin
D001798:Blood Proteins; D011480:Protease Inhibitors; D000515:alpha 1-Antitrypsin; D002918:Chymotrypsin; D014357:Trypsin