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|Title:||Characterization of polyphenol oxidase from aerial roots of an orchid, Aranda 'Christine 130'|
Polyphenol oxidase isoforms
Temperature phase partitioning
|Citation:||Ho, 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|
|Abstract:||Four 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.|
|Source Title:||Plant Physiology and Biochemistry|
|Appears in Collections:||Staff Publications|
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