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The biological incorporation of purines and pyrimidines into nucleosides and nucleic acid

The biological incorporation of purines and pyrimidines into nucleosides and nucleic acid

Biochimica et Biophysica Acta 4(1-3): 232-237

A critical review. The mechanism of incorporation of purines and pyrimidines into ribosidic linkage was discussed. The enzyme catalyzing the equilibrium: ribose-1-phosphate+ hypoxathine[image]inosine + inorganic phosphate was called nucleoside phosphorylase (I). In an enzymatic mixture of free purine, phosphate, nucleoside and phospho-riboside, the equilibrium was favorable for nucleoside formation. I, was obtained from liver and possessed a certain specificity with regard to the nitrogenous bases and to the pentoses. Inosine and guanine riboside were the only ribosides which underwent phosphorolysis in the presence of enzyme used. Adenosine, xanthosine and pyrimidine ribosides were inert. Only the furanoid, not the py-ranoid, pentose was effective. Hexoses did not react. A parallel enzyme system which catalysed the phosphorolysis of desoxyribo-sides was also demonstrated in vitro. A new phosphoric ester, obtained from incubating guanine desoxyriboside with I, was believed to be desoxyribose-1-phosphate (II). At 25", pH 4, 50% of II was split into inorganic phosphate and sugar in 11 min. Crude I fractionated by various means catalyzes the phosphorolysis of purine ribosides as well as desoxyribosides. It was assumed that the same enzyme acted in both systems. From in vivo studies using tracer technique by various authors it was found: (1) N15-labelled guanine or hypoxanthine was converted exclusively into uric acid and allantoin and no N15 was detected in nucleic acid; (2) adenine was readily incorporated into ribonucleic acids both as adenine and guanine; and (3) 2,6-diaminopurine appeared in large amt. in the nucleic acid guanine but not in the adenine. The apparent controversy between these findings and the action of I was explained with various ways.

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Accession: 025690288

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PMID: 15403929

DOI: 10.1016/0006-3002(50)90029-1

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