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Dried extracts of woolly aphid were treated with n-butanol, then by chromatography on DEAESephadex A50 and finally by filtration on Sephadex G150 to yield a substantially homogeneous protein catalysing the conversion of the aglucone of protoaphin into xanthoaphin. Traces of lowmolecular- weight contaminants were removed by chromatography on Sephadex G 100. The enzyme, which has a molecular weight of 1200002000 and a high content of p-structure, was inhibited by naphthoresorcinol. Its glycoprotein nature was indicated by amino acid analysis.

australian journal of biological sciences

Colouring Matters of the Aphidoidea XLII. Purification and Properties of the Cyclising Enzyme [Protoaphin Dehydratase (Cyclising)] Concerned with Pigment Transformations in the Woolly Aphid Eriosoma lanigerum Hausmann (Hemiptera: Insecta)