Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0981-9428(99)00114-X
DC FieldValue
dc.titleCharacterization of polyphenol oxidase from aerial roots of an orchid, Aranda 'Christine 130'
dc.contributor.authorHo, K.-K.
dc.date.accessioned2014-10-27T08:23:39Z
dc.date.available2014-10-27T08:23:39Z
dc.date.issued1999-11
dc.identifier.citationHo, K.-K. (1999-11). Characterization of polyphenol oxidase from aerial roots of an orchid, Aranda 'Christine 130'. Plant Physiology and Biochemistry 37 (11) : 841-848. ScholarBank@NUS Repository. https://doi.org/10.1016/S0981-9428(99)00114-X
dc.identifier.issn09819428
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100246
dc.description.abstractFour isoforms of polyphenol oxidase (PPO) were demonstrated in the aerial roots of a tropical orchid, Aranda 'Christine 130'. They were extracted at neutral pH and purified to homogeneity as judged by SDS-gel electrophoresis. Purification was achieved by a combination of Triton X-114 treatment, temperature phase partitioning, gel filtration chromatography, ion-exchange separation and chromatofocusing. Two of the isoforms, designated PPO(a) and PPO(d), differed in their N-terminal sequence, tryptic peptide map and substrate affinity for (+)-catechin, but exhibited similarity in their molecular mass under denaturing conditions, pH optimum and kinetic behaviour toward 4-methyl catechol. The other two isoforms, PPO(b) and PPO(c), were identical to PPO(a) and PPO(d), respectively, in terms of their N-terminal sequence, substrate preference and pH maximum, but were different with regard to their molecular mass under denaturing conditions. These four isoforms differed in their isoelectric point.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0981-9428(99)00114-X
dc.sourceScopus
dc.subjectAerial roots
dc.subjectArachnis hookerana
dc.subjectChromatofocusing
dc.subjectNeutral pH
dc.subjectPolyphenol oxidase isoforms
dc.subjectTemperature phase partitioning
dc.subjectTriton X-114
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/S0981-9428(99)00114-X
dc.description.sourcetitlePlant Physiology and Biochemistry
dc.description.volume37
dc.description.issue11
dc.description.page841-848
dc.description.codenPPBIE
dc.identifier.isiut000084478800005
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