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dc.creatorBozic, NA
dc.creatorVujčić, Zoran
dc.date.accessioned2018-11-22T00:08:29Z
dc.date.available2018-11-22T00:08:29Z
dc.date.issued2005
dc.identifier.issn0173-0835
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/714
dc.description.abstractA general method for detecting leucyl aminopeptidase activity after native polyacrylamide gel electrophoresis (PAGE) in situ is described. The method is based on diazotization of p-nitroaniline, liberated in the polyacrylamide gel by leucyl aminopeptidase action on leucine-p-nitroanilide (LpNA) and subsequent coupling with a chromogen, 1-naphthylamine, until a pink azo dye product at the position of enzyme activity is obtained. A possible use of this technique for leucyl aminopeptidase detection and quantification is indicated. This method was found to be reproducible with the coefficient of variation below 15% for a 32-fold range, while the colored area of enzyme activity was in linear dependence to enzyme activity. Applications of this method with some other aminoacyl-p-nitroanilides and for detection of kidney bean leucyl aminopeptidase isoforms are demonstrated.en
dc.publisherWiley-V C H Verlag Gmbh, Weinheim
dc.rightsrestrictedAccess
dc.sourceElectrophoresis
dc.subjectisoenzymesen
dc.subjectleucyl aminopeptidaseen
dc.subjectPhaseolus vulgarisen
dc.subjectp-nitroanilideen
dc.subjectzymogramen
dc.titleDetection and quantification of leucyl arninopeptidase after native electrophoresis using leucine-p-nitroanilideen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractБозиц, НA; Вујчић, Зоран;
dc.citation.volume26
dc.citation.issue12
dc.citation.spage2476
dc.citation.epage2480
dc.identifier.wos000230239900022
dc.identifier.doi10.1002/elps.200500047
dc.citation.other26(12): 2476-2480
dc.citation.rankaM21
dc.identifier.pmid15920779
dc.type.versionpublishedVersionen
dc.identifier.scopus2-s2.0-21644465014
dc.identifier.rcubKon_1667


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