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dc.contributorWichita State University. Department of Chemistryen_US
dc.contributor.authorGroutas, William C.en_US
dc.contributor.authorHouser-Archield, Nadeneen_US
dc.contributor.authorChong, Lee S.en_US
dc.contributor.authorVenkataraman, Radhikaen_US
dc.contributor.authorEpp, Jeffrey B.en_US
dc.contributor.authorHuang, Heen_US
dc.contributor.authorMcClenahan, Jerald J.en_US
dc.identifierHL 38048en_US
dc.identifier.citationJournal of medicinal chemistry. 1993 Oct 15; 36(21): 3178-81.en_US
dc.descriptionFull text of this article is not available in SOAR.en_US
dc.description.abstractA series of saccharin derivatives I has been synthesized and evaluated for their inhibitory activity toward human leukocyte elastase and cathepsin G. Most of the compounds were found to be efficient and time-dependent inhibitors of elastase. Inactivated elastase was found to regain its activity almost fully after 24 h (80-90% activity) and the half-lives of reactivation ranged between 12-15 h. Addition of hydroxylamine to fully-inactivated enzyme led to rapid and complete recovery of enzymatic activity. A tentative mechanism of action is proposed on the basis of biochemical and model studies.en_US
dc.description.sponsorshipNHLBI NIH HHSen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofseriesJournal of medicinal chemistryen_US
dc.relation.ispartofseriesJ. Med. Chem.en_US
dc.subjectResearch Support, U.S. Gov't, P.H.S.en_US
dc.subject.meshCathepsin Gen_US
dc.subject.meshCathepsins/antagonists & inhibitorsen_US
dc.subject.meshLeukocyte Elastaseen_US
dc.subject.meshPancreatic Elastase/antagonists & inhibitorsen_US
dc.subject.meshSaccharin/analogs & derivativesen_US
dc.subject.meshSerine Endopeptidasesen_US
dc.subject.meshStructure-Activity Relationshipen_US
dc.titleEfficient inhibition of human leukocyte elastase and cathepsin G by saccharin derivativesen_US
dc.coverage.spacialUnited Statesen_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright © 1993 American Chemical Societyen_US

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