Abstract
THE N-6 substituted adenines with a lipophilic radical show a biological activity of the kinetin type1,2. The ribosides of substituted adenine present an activity at least identical to that of the free bases2,3; this could be possibly attributed to their hydrolysis and the subsequent formation of the free bases. To test this hypothesis, the action of nucleoside phosphorylase from Escherichia coli was analysed on the ribosides of two kinins: 6-benzylaminopurine and 6-hexylaminopurine. The method used for the enzyme preparation was that of Paege and Schlenk4; the fraction of protein precipitated with ammonium sulphate between 60 and 80 per cent of saturation was retained and then dialysed. Preliminary tests on the hydrolysis of nucleosides were effected with inosine and adenosine.
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References
Kuraishi, S., Sci. Papers Coll. Gen. Educ., Univ. Tokyo, 9, 67 (1959).
Strong, F. M., Topics Microbial. Chem. (John Wiley, New York, 1956).
Guern, J., and Hugon, E., C. R. Acad. Sci. (in the press).
Paege, L. M., and Schlenk, F., Arch. Biochem. Biophys., 40, 42 (1952).
Kalckar, H. M., J. Biol. Chem., 167, 429 (1947).
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TROUSLOT, M., GUERN, J. Enzyme Hydrolysis of 6-Benzylamino-9B D-Ribofuranosylpurine and 6-Hexylamino-9B D-Ribofuranosylpurine. Nature 213, 629–630 (1967). https://doi.org/10.1038/213629a0
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DOI: https://doi.org/10.1038/213629a0
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