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Science 17 November 1978:
Vol. 202. no. 4369, pp. 757 - 760
DOI: 10.1126/science.715439
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Articles

Science, Vol 202, Issue 4369, 757-760
Copyright © 1978 by American Association for the Advancement of Science

articles

S-adenosylhomocysteine hydrolase is an adenosine-binding protein: a target for adenosine toxicity

MS Hershfield and NM Krodich

When adenosine deaminase activity is inhibited, low concentrations of adenosine are toxic to human lymphoblast mutants that are unable to convert adenosine to intracellular nucleotides. In order to identify the mediator of this cytotoxicity, we searched for a cytoplasmic protein capable of binding adenosine with high affinity. Such a protein was identified in extracts of human lymphoblasts and placenta as the enzyme S-adenosylhomocysteine hydrolase.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Localization of S-adenosylhomocysteine Hydrolase in the Rat Kidney.
D. Kloor, W. Stumvoll, H. Schmid, J. Kömpf, A. Mack, and H. Osswald (2000)
J. Histochem. Cytochem. 48, 211-218
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Nuclear Accumulation of S-Adenosylhomocysteine Hydrolase in Transcriptionally Active Cells during Development of Xenopus laevis.
N. Radomski, C. Kaufmann, and C. Dreyer (1999)
Mol. Biol. Cell 10, 4283-4298
   Abstract »    Full Text »
2'-Deoxycoformycin (Pentostatin) for Lymphoid Malignancies: Rational Development of an Active New Drug.
P. J. O'DWYER, B. WAGNER, B. LEYLAND-JONES, R. E. WITTES, B. D. CHESON, and D. F. HOTH (1988)
Ann Intern Med 108, 733-743
   Abstract »    PDF »
The human genes for S-adenosylhomocysteine hydrolase and adenosine deaminase are syntenic on chromosome 20.
M. Hershfield and U Francke (1982)
Science 216, 739-742
   Abstract »    PDF »


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