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Purification and Properties of the diamine oxidase of pea seedlings

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dc.contributor.authorDeveci, Nuran
dc.contributor.authorGüvenilir, Yüksel A.
dc.date.accessioned2026-01-26T01:16:09Z
dc.date.issued1995-04-01
dc.description.abstractEnzymes have been used extensively in many industries for the last 20 yrs. The purpose of this study was the isolation, purification, and specification of diamine oxidase (DAO) of pea seedlings. The relationship between enzyme activity and growth conditions has been investigated. DAO that was extracted from pea seedlings was purified by centrifugation, thermal denaturation, fractionation with ammonium sulfate, precipitation of inert components, column electrophoresis, and DEAE-cellulose column chromatography. It was found that the final enzyme preparation is 400-fold purer than the original extract at the end of the purification steps. The molecular weight, isoelectric point, and copper content of the purified enzyme also were determined.
dc.description.urihttps://doi.org/10.1007/bf02783484
dc.description.urihttps://dx.doi.org/10.1007/bf02783484
dc.identifier.doi10.1007/bf02783484
dc.identifier.eissn1559-0291
dc.identifier.endpage90
dc.identifier.issn0273-2289
dc.identifier.openairedoi_dedup___::b8d16baba4dc0c230c1016358d6b5d91
dc.identifier.startpage83
dc.identifier.urihttps://hdl.handle.net/11527/55726
dc.identifier.volume53
dc.language.isoeng
dc.publisherSpringer Science and Business Media LLC
dc.relation.ispartofApplied Biochemistry and Biotechnology
dc.rightsCLOSED
dc.titlePurification and Properties of the diamine oxidase of pea seedlings
dc.typeArticle
dspace.entity.typePublication

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