Cinnabarinic Acid Formation in Malpighian Tubules of the Silkworm,Bombyx mori.Participation of Catalase in Cinnabarinic Acid Formation in the Presence of Manganese Ion

Publisher Website
Google Scholar
Abstract
Cinnabarinic acid was formed from 3-hydroxyanthranilic acid during incubation with a soluble fraction from Malpighian tubules of the silkworm, B. mori, in the presence of Mn2+. The enzyme having this activity was purified to homogeneity by ammonium sulfate fractionation, gel filtration and ion exchange chromatography. Enzyme activity was accompanied by parallel catalase activity at all steps of purification; the 2 activities could not be separated from each other. The purified protein was concluded to be catalase. Mg2+ was shown to be present in 0.1 mM concentration of Malpighian tubules of B. mori. In the Malpighian tubules catalase participates in the formation of cinnabarinic acid. A possible mechanism for the formation of cinnabarinic acid from 3-hydroxyanthranilic acid by catalase in the presence of Mg2+ is proposed.