Abstract
The berberine bridge-forming enzyme (BBE) has been found in 66 samples taken from differentiated plants and from cell suspension cultures. It was purified 450-fold from Berberis beaniana cell cultures by gel-filtration, DEAE and phenyl-Sepharose chromatography, electrophoresis and isoclectric focusing. The enzyme was shown to be homogeneous by gel electrophoresis ( M r = 52 kD ± 4). The enzyme, which requires the presence of oxygen, catalyses the conversion of the ( S)-enantiomers of reticuline, protosinomenine and laudanosoline to the corresponding ( S)-tetrahydroprotoberberines and released stoichiometric amounts of H 2O 2. Within the cells the enzyme is located in a particle with the density p = 1.14 g/ml.
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