6533b830fe1ef96bd12972b1
RESEARCH PRODUCT
Hydroquinone: O-glucosyltransferase from cultivated Rauvolfia cells: enrichment and partial amino acid sequences.
Joachim ArendHeribert WarzechaJoachim Stöckigtsubject
RauvolfiaStereochemistryMolecular Sequence DataPeptidePlant ScienceHorticultureBiochemistryRauwolfiachemistry.chemical_compoundRauvolfia serpentinaAmino Acid SequenceMolecular BiologyCells Culturedchemistry.chemical_classificationChromatographyPlants MedicinalbiologyChromatofocusingArbutinGeneral Medicinebiology.organism_classificationChromatography Ion ExchangePeptide FragmentsAmino acidMolecular WeightKineticsEnzymeDurapatitechemistryBiochemistryGlucosyltransferasesbiology.proteinGlucosyltransferaseElectrophoresis Polyacrylamide Geldescription
Plant cell suspension cultures of Rauvolfia are able to produce a high amount of arbutin by glucosylation of exogenously added hydroquinone. A four step purification procedure using anion exchange, hydrophobic interaction, hydroxyapatite-chromatography and chromatofocusing delivered in a yield of 0.5%, an approximately 390 fold enrichment of the involved glucosyltransferase. SDS-PAGE showed a M(r) for the enzyme of 52 kDa. Proteolysis of the pure enzyme with endoproteinase LysC revealed six peptide fragments with 9-23 amino acids which were sequenced. Sequence alignment of the six peptides showed high homologies to glycosyltransferases from other higher plants.
year | journal | country | edition | language |
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2000-02-19 | Phytochemistry |