Isolation and partial characterization of an elastase-type enzyme from human arterial wall by lima-bean trypsin inhibitor affinity chromatography.
A serine protease active on insoluble elastin at neutral pH has been isolated from human aortic media employing a Lima-bean trypsin inhibitor - Sepharose column. It is also hydrolyzed Suc (Ala)3 pna and casein but was found inactive against Benzoyl-Tyr-pna and Benzoyl-Arg-pna. Its apparent molecular weight as determined by SDS-PAGE was 22,300 Daltons. It differs from other elastases of human origin (human pancreatic elastase-1, human pancreatic elastase-2, human leucocyte elastase) on the basis of amino-acid composition and immunological specificity.
D000596:Amino Acids / Q000032:analysis; D001011:Aorta / Q000201:enzymology*; D002846:Chromatography, Affinity / Q000379:methods*; D004549:Elastin / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D010196:Pancreatic Elastase / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
D000596:Amino Acids; D004549:Elastin; D010196:Pancreatic Elastase