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Science 23 September 1977:
Vol. 197. no. 4310, pp. 1284 - 1287
DOI: 10.1126/science.197600
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Articles

Science, Vol 197, Issue 4310, 1284-1287
Copyright © 1977 by American Association for the Advancement of Science

articles

Adenine and adenosine are toxic to human lymphoblast mutants defective in purine salvage enzymes

MS Hershfield, FF Snyder, and JE Seegmiller

Mutants deficient in adenosine kinase or adenine phosphoribosyltransferase activities were selected from the WI-L2 line of human lymphoblasts. The adenosine kinase-deficient mutant was still as sensitive as its parent to growth inhibition caused by adenosine deaminase was inhibited. Similarly, the adenine phosphoribosyltransferase mutant remained sensitive to growth inhibition caused by adenine. Thus, the toxicity of adenine and adenosine to human lymphoblasts is not mediated by nucleotides to which they may be converted.


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Amidophosphoribosyltransferase Limits the Rate of Cell Growth-linked de Novo Purine Biosynthesis in the Presence of Constant Capacity of Salvage Purine Biosynthesis.
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Purinogenic Immunodeficiency Diseases: Clinical Features and Molecular Mechanisms.
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S-adenosylhomocysteine hydrolase is an adenosine-binding protein: a target for adenosine toxicity.
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Science 202, 757-760
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