ISOLATION AND PARTIAL CHARACTERIZATION OF AN ELASTASE-TYPE ENZYME FROM HUMAN ARTERIAL-WALL BY LIMA-BEAN TRYPSIN-INHIBITOR AFFINITY-CHROMATOGRAPHY
- 1 January 1980
- journal article
- research article
- Vol. 7 (4) , 290-302
Abstract
A serine protease active on insoluble elastin at neutral pH was isolated from human aortic media employing a Lima-bean trypsin inhibitor-Sepharose column. It hydrolyzed Suc(Ala)3 pna and casein but was found inactive against Benzoyl-Tyr-pna [paranitroanilide] and Benzoyl-Arg-pna. Its apparent MW 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 leukocyte elastase) on the basis of aminoacid composition and imunological specificity.This publication has 6 references indexed in Scilit:
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