An enzyme catalyzing the ribosyl group transfer from inosine to adenine was purified from Aerobacter cloacae No. 172–1 by means of ammonium sulfate fractionation and DEAE-cellulose and hydroxylapatite column chromatographies. A. cloacae was found to have much activities of this enzyme in its cell free extract. The enzyme activity was increased about 90-fold. By using the purified enzyme, some properties of the reaction were investigated. The enzyme was considerably stable and essentially required inorganic orthophosphate for the reaction. It was suggested that the enzyme might be a purine nucleoside phosphorylase and that the reaction might be a coupled reaction with ribose-1-phosphate as an intermediate. The enzyme could not transfer the ribosyl group between purine and pyrimidine bases.
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Tazuke et al. (1963) studied this question.