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关于苏拉明介导的对细胞和病毒DNA聚合酶抑制作用的观察

Observations on the suramin-mediated inhibition of cellular and viral DNA polymerases.

作者信息

Basu A, Modak M J

出版信息

Biochem Biophys Res Commun. 1985 May 16;128(3):1395-402. doi: 10.1016/0006-291x(85)91095-2.

DOI:10.1016/0006-291x(85)91095-2
PMID:2408617
Abstract

We have examined the sensitivity of various cellular and viral DNA polymerases to Suramin, an antitrypanosomal drug, which has been reported to exhibit antireverse transcriptase activity. We find that Suramin is a nonspecific inhibitor of all the viral and cellular DNA polymerases, including terminal deoxynucleotidyl transferase, and that the inhibition is most readily reversed by the addition of serum albumin. The drug appears to bind to all the enzyme proteins with no apparent selectivity. Binding of Suramin to enzyme has been found to result in the loss of both substrate and templateprimer binding abilities of various enzymes, confirming the nonspecific nature of protein-Suramin interaction.

摘要

我们研究了多种细胞和病毒DNA聚合酶对苏拉明(一种抗锥虫药物,据报道具有抗逆转录酶活性)的敏感性。我们发现,苏拉明是所有病毒和细胞DNA聚合酶(包括末端脱氧核苷酸转移酶)的非特异性抑制剂,并且通过添加血清白蛋白,这种抑制作用最容易被逆转。该药物似乎无明显选择性地与所有酶蛋白结合。已发现苏拉明与酶的结合会导致各种酶的底物和模板引物结合能力丧失,这证实了蛋白质 - 苏拉明相互作用的非特异性性质。

相似文献

1
Observations on the suramin-mediated inhibition of cellular and viral DNA polymerases.关于苏拉明介导的对细胞和病毒DNA聚合酶抑制作用的观察
Biochem Biophys Res Commun. 1985 May 16;128(3):1395-402. doi: 10.1016/0006-291x(85)91095-2.
2
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3'-Hydroxymethyl 2'-deoxynucleoside 5'-triphosphates are inhibitors highly specific for reverse transcriptase.3'-羟甲基2'-脱氧核苷5'-三磷酸是对逆转录酶具有高度特异性的抑制剂。
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Stereospecificity of human DNA polymerases alpha, beta, gamma, delta and epsilon, HIV-reverse transcriptase, HSV-1 DNA polymerase, calf thymus terminal transferase and Escherichia coli DNA polymerase I in recognizing D- and L-thymidine 5'-triphosphate as substrate.人DNA聚合酶α、β、γ、δ和ε、HIV逆转录酶、单纯疱疹病毒1型DNA聚合酶、小牛胸腺末端转移酶及大肠杆菌DNA聚合酶I在识别D-和L-胸腺嘧啶核苷5'-三磷酸作为底物时的立体特异性。
Nucleic Acids Res. 1995 Aug 11;23(15):2840-7. doi: 10.1093/nar/23.15.2840.

引用本文的文献

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Proc Natl Acad Sci U S A. 1986 Sep;83(17):6440-4. doi: 10.1073/pnas.83.17.6440.
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