Studies on the biosynthesis of cyclitols, XXXIV[l] Purification of myo-inositol 3-methyltransferase from Pisum sativum and of myo-inositol 1-methyltransferase from Vinca minor to homogeneity by affinity chromatography.

With the help of affinity chromatography on an agarose gel containing epi-inositol as the group exhibiting affinity towards enzymes acting on myo-inositol, the two methyltransferases from higher plant materials transforming myo-inositol to D-bornesitol and L-bornesitol, respectively, were purified to homogeneity. The two enzymes show certain similarities as far as pH optima, isoelectric points and specific activities are concerned, but differ significantly in the molecular weight and in their affinity towards the methyl donor, S-adenosyl-L-methionine.