Abstract
(S)-Tetrahydroberberine (THB) oxidase was purified to homogeniety from cultured Coptis japonica cells by DEAE-Sepharose chromatography, gel filtration, and HPLC. The enzyme catalysed the removal of four hydrogen atoms from one mol of (S)-THB and produced two mol of hydrogen peroxide and one mol of berberine in the presence of molecular oxygen. The purified enzyme had neither the yellow fluoresence characteristic of flavin derivatives nor an absorption spectrum showing the presence of haem. The enzyme had a Mr of 58 000 and consisted of two identical subunits of 28 000 each.
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