Compounds > 3--azido-3--deoxythymidine-5-phosphate

3--azido-3--deoxythymidine-5-phosphate and Leukemia-L1210

3--azido-3--deoxythymidine-5-phosphate has been researched along with Leukemia-L1210* in 1 studies

Other Studies

1 other study(ies) available for 3--azido-3--deoxythymidine-5-phosphate and Leukemia-L1210

Article	Year
Interaction of the 5'-phosphates of the anti-HIV agents, 3'-azido-3'-deoxythymidine and 3'-azido-2',3'-dideoxyuridine, with thymidylate synthase. Biochemical and biophysical research communications, 1988, Sep-30, Volume: 155, Issue:3 A study has been made of the interaction of 3'-azido-3'-deoxythymidine 5'-phosphate (AZTMP) and 3'-azido-2',3'-dideoxy-uridine 5'-phosphate (AZdUMP) with thymidylate synthase. With the enzyme from L1210 cells and the tapeworm Hymenolepis diminuta, AZTMP was a weak inhibitor competitive with respect to dUMP (Ki = 6.3 mM and 0.5 mM); hence cytotoxicity of AZT, in cells in which accumulation of AZTMP is not high, is not due to inhibition of cellular thymidylate synthase. AZdUMP, with the L1210 enzyme, was a weak substrate (competition with dUMP described by apparent Ki = 4.7 mM), excluding conversion of AZdUMP to AZTMP as a source of toxicity of 3'-azido-2',3'-dideoxyuridine. An efficient procedure is described for enzymatic phosphorylation on a preparative scale of dideoxynucleosides. Topics: Animals; Antiviral Agents; Dideoxynucleotides; Hymenolepis; Leukemia L1210; Thymidylate Synthase; Thymine Nucleotides; Zidovudine	1988

Article

Year

Interaction of the 5'-phosphates of the anti-HIV agents, 3'-azido-3'-deoxythymidine and 3'-azido-2',3'-dideoxyuridine, with thymidylate synthase.

Biochemical and biophysical research communications, 1988, Sep-30, Volume: 155, Issue:3

A study has been made of the interaction of 3'-azido-3'-deoxythymidine 5'-phosphate (AZTMP) and 3'-azido-2',3'-dideoxy-uridine 5'-phosphate (AZdUMP) with thymidylate synthase. With the enzyme from L1210 cells and the tapeworm Hymenolepis diminuta, AZTMP was a weak inhibitor competitive with respect to dUMP (Ki = 6.3 mM and 0.5 mM); hence cytotoxicity of AZT, in cells in which accumulation of AZTMP is not high, is not due to inhibition of cellular thymidylate synthase. AZdUMP, with the L1210 enzyme, was a weak substrate (competition with dUMP described by apparent Ki = 4.7 mM), excluding conversion of AZdUMP to AZTMP as a source of toxicity of 3'-azido-2',3'-dideoxyuridine. An efficient procedure is described for enzymatic phosphorylation on a preparative scale of dideoxynucleosides.

Topics: Animals; Antiviral Agents; Dideoxynucleotides; Hymenolepis; Leukemia L1210; Thymidylate Synthase; Thymine Nucleotides; Zidovudine

1988