PURIFICATION AND PROPERTIES OF A BACTERIAL DEOXYRIBOSE TRANSFERASE
1959 Volume 46 Issue 6 Pages 725-732
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1959 Volume 46 Issue 6 Pages 725-732
1. Deoxyribose transferase has been purified about 20-fold from the extract of Lactobacillus delbrueckii. With the purified enzyme preparation no evidence for phosphate requirement has been found.
2. The enzyme catalyzes a reversible reaction: with initially equimolar quantities of pyrimidine deoxyriboside and adenine, at equilibrium about 80 per cent of the total deoxyribose is present as purine derivatives, and the content increases with the elevated levels of adenine added as acceptor of the deoxyribosyl group. A considerable number of purine bases participate in this transfer reaction.
3. The possibility that the deoxyribosyl group of pyrimidine deoxyri-bosides could be determined or isolated using this enzyme is discussed.
The authors wish to express their appreciation Dr. B. L. Horecker of the National Instintes of Health, Bethesda, Haryland and to Prof. K. Ichihara for his interest and encouragement in this work.
This work was supported by a grant for Fundamental Scientific Research of the Ministry of Education.
