Effect of different elastase inhibitors on leukocyte elastase pre-adsorbed to elastin.
The effect of three elastase inhibitors (MeO-Suc-Ala-Ala-Pro-Val-CH2Cl, eglin c and alpha 1-proteinase inhibitor) on the hydrolysis of [3H]elastin was determined. The low-molecular mass inhibitors inactivated elastase nearly completely, regardless of whether or not the enzyme was adsorbed to its substrate elastin prior to the addition of the inhibitors. In contrast, elastase preadsorbed to elastin was much less sensitive to the inhibitory effect of alpha 1-proteinase inhibitor than the free elastase.
D004549:Elastin; D004800:Enzymes, Immobilized / Q000037:antagonists & inhibitors*; D006801:Humans; D007700:Kinetics; D007962:Leukocytes / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D011480:Protease Inhibitors / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D004800:Enzymes, Immobilized; D011480:Protease Inhibitors; D004549:Elastin; D010196:Pancreatic Elastase