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Two S-adenosyl-ʟ-methionine:furanocoumarin O-methyltransferases of R . graveolens, acting at the 5-and 8-hydroxyls of the psoralen nucleus, were completely resolved by adsorption on a general affinity ligand, 5 -(3-carboxypropanamido) xanthotoxin, followed by specific desorption by bergaptol and xanthotoxol, respectively. The 5-O-methyltransferase was purified 450-fold by this procedure, the 8-O-methyltransferase 112-fold, and both enzyme fractions were electrophoretically homogeneous. No resolution could be achieved of the activity against two 5-hydroxypsoralens or of the activity against two 8-hydroxypsoralens, and conclusive evidence is presented for the existence of only one 5-O-methyltransferase and only one 8-O-methyltransferase acting on linear furanocoumarins.

zeitschrift für naturforschung c

Separation of the S-Adenosylmethionine: 5-and 8-Hydroxyfuranocoumarin O-Methyltransferases of Ruta graveolens L. by General Ligand Affinity Chromatography