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- Daniel V. Santi
- Department of Chemistry, University of California, Santa Barbara, Santa Barbara, Calif. 93106
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- Charles S. McHenry
- Department of Chemistry, University of California, Santa Barbara, Santa Barbara, Calif. 93106
抄録
<jats:p>5-Fluoro-2′-deoxyuridylate causes a rapid inactivation of thymidylate synthetase that is dependent upon prior complexation of the cofactor 5,10-methylenetetrahydrofolate. The enzyme-5-fluoro-2′-deoxyuridylate complex may be isolated on nitrocellulose membranes and is not disrupted by 6 M urea. Upon reaction of 5-fluoro-2′-deoxyuridylate with the enzyme in the presence of 5,10-methylenetetrahydrofolate a rapid loss of absorbance is observed at 269 nm, the absorption maximum for the pyrimidine chromophore. It is concluded that a covalent bond is formed between the 6-position of 5-fluoro-2′-deoxyuridylate and a nucleophilic group of the enzyme that is involved in catalysis.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 69 (7), 1855-1857, 1972-07
Proceedings of the National Academy of Sciences
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詳細情報
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- CRID
- 1361981470479872384
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- NII論文ID
- 30016259709
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- ISSN
- 10916490
- 00278424
- http://id.crossref.org/issn/00278424
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- データソース種別
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- Crossref
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