Purification of alcohol dehydrogenase from four genotypes of the olive fruit fly Bactrocera (Dacus) oleae

dc.contributor.author	Mazi, VE	en
dc.contributor.author	Cosmidis, N	en
dc.contributor.author	Clonis, YD	en
dc.contributor.author	Loukas, M	en
dc.date.accessioned	2014-06-06T06:43:39Z
dc.date.available	2014-06-06T06:43:39Z
dc.date.issued	1998	en
dc.identifier.issn	87567938	en
dc.identifier.uri	http://dx.doi.org/10.1021/bp970114n	en
dc.identifier.uri	http://62.217.125.90/xmlui/handle/123456789/1424
dc.subject.other	affinity chromatography	en
dc.subject.other	Bactrocera oleae	en
dc.subject.other	enzyme analysis	en
dc.subject.other	enzyme purification	en
dc.subject.other	genotype	en
dc.subject.other	high performance liquid chromatography	en
dc.subject.other	ion exchange chromatography	en
dc.subject.other	molecular weight	en
dc.subject.other	precipitation	en
dc.subject.other	SDS polyacrylamide gel electrophoresis	en
dc.subject.other	Affinity chromatography	en
dc.subject.other	Ammonium compounds	en
dc.subject.other	Dyes	en
dc.subject.other	High performance liquid chromatography	en
dc.subject.other	Ion exchange	en
dc.subject.other	Purification	en
dc.subject.other	Alcohol dehydrogenase	en
dc.subject.other	Ammonium sulfate	en
dc.subject.other	Enzymes	en
dc.subject.other	Alcohol Dehydrogenase	en
dc.subject.other	Animals	en
dc.subject.other	Diptera	en
dc.subject.other	Electrophoresis, Polyacrylamide Gel	en
dc.subject.other	Genotype	en
dc.subject.other	Linear Models	en
dc.subject.other	Molecular Weight	en
dc.subject.other	Time Factors	en
dc.subject.other	Bactrocera oleae	en
dc.subject.other	Drosophila melanogaster	en
dc.subject.other	Oleaceae	en
dc.title	Purification of alcohol dehydrogenase from four genotypes of the olive fruit fly Bactrocera (Dacus) oleae	en
heal.type	journalArticle	en
heal.identifier.primary	10.1021/bp970114n	en
heal.publicationDate	1998	en
heal.abstract	This is the first report describing the purification of alcohol dehydrogenase (ADH) from four genotypes of the olive fruit fly Bactrocera oleae, the most important pest of olives in the Mediterranean region. The purified enzyme shows a single band after SDS-PAGE analysis, corresponding to subunit mass of 26 kDa. The native ADH shows a molecular mass of 48 kDa, after gel filtration HPLC analysis. The purification method incorporated a preliminary ammonium sulphate precipitation step, followed by an anion-exchange DEAE chromatography step, a dye affinity chromatography step on Cibacron blue 3GA, and an anion-exchange DEAE chromatography step employing the same column of the first step. The present method offers good overall recovery (40%) and high enzyme purity, and it is applicable to different genotypes. Furthermore, the method is rapid and economical, as it employs two cheap, widely used, and commercially available chromatography materials.This is the first report describing the purification of alcohol dehydrogenase (ADH) from four genotypes of the olive fruit fly Bactrocera oleae, the most important pest of olives in the Mediterranean region. The purified enzyme shows a single band after SDS-PAGE analysis, corresponding to subunit mass of 26 kDa. The native ADH shows a molecular mass of 48 kDa, after gel filtration HPLC analysis. The purification method incorporated a preliminary ammonium sulphate precipitation step, followed by an anion-exchange DEAE chromatography step, a dye affinity chromatography step on Cibacron blue 3GA, and an anion-exchange DEAE chromatography step employing the same column of the first step. The present method offers good overall recovery (40%) and high enzyme purity, and it is applicable to different genotypes. Furthermore, the method is rapid and economical, as it employs two cheap, widely used, and commercially available chromatography materials.	en
heal.publisher	AIChE, New York, NY, United States	en
heal.journalName	Biotechnology Progress	en
dc.identifier.issue	2	en
dc.identifier.volume	14	en
dc.identifier.doi	10.1021/bp970114n	en
dc.identifier.spage	294	en
dc.identifier.epage	299	en