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dc.contributor.authorDemir, Dudu
dc.contributor.authorGençer, Nahit
dc.contributor.authorEr, Aylin
dc.date.accessioned2019-10-17T11:42:48Z
dc.date.available2019-10-17T11:42:48Z
dc.date.issued2012en_US
dc.identifier.issn1073-1199
dc.identifier.urihttps://doi.org/10.3109/10731199.2012.696060
dc.identifier.urihttps://hdl.handle.net/20.500.12462/8703
dc.descriptionGençer, Nahit (Balikesir Author)en_US
dc.description.abstractProphenoloxidase (PPO) was purified from Galleria mellonella L. A 67-fold purification of the proenzyme with 352% yield was achieved by using a Sepharose 4B-L-tyrosine-p-amino benzoic acid affinity column. The purified enzyme was migrated as a single band on SDS-polyacrylamide gel electrophoresis. Km and V-max values were 0.017 M and 1430.45 EU for catechol. Inhibition of PPO was investigated with inhibitors such as p-aminobenzoic acid, etyleneglycol, and ascorbic acid. Among them, ascorbic acid showed the strongest inhibitory activity with IC50 value of 2.94 mu M. The current paper represents new strategies for the biological control of the Galleria mellonella L. insect.en_US
dc.language.isoengen_US
dc.publisherInforma Healthcareen_US
dc.relation.isversionof10.3109/10731199.2012.696060en_US
dc.rightsinfo:eu-repo/semantics/embargoedAccessen_US
dc.subjectGalleria Mellonellaen_US
dc.subjectProphenol Oxidaseen_US
dc.subjectAffinity Chromatographyen_US
dc.subjectInhibitionen_US
dc.titlePurification and characterization of prophenoloxidase from Galleria mellonella L.en_US
dc.typearticleen_US
dc.relation.journalArtificial Cells Blood Substitutes and Biotechnologyen_US
dc.contributor.departmentFen Edebiyat Fakültesien_US
dc.contributor.authorID0000-0001-7092-8857en_US
dc.identifier.volume40en_US
dc.identifier.issue6en_US
dc.identifier.startpage391en_US
dc.identifier.endpage395en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US


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