...
首页> 外文期刊>Journal of Virology >Neutralization of herpes simplex virus ribonucleotide reductase activity by an oligopeptide-induced antiserum directed against subunit H2.
【24h】

Neutralization of herpes simplex virus ribonucleotide reductase activity by an oligopeptide-induced antiserum directed against subunit H2.

机译:通过针对亚基H2的寡肽诱导的抗血清中和疱疹病毒核糖核苷酸还原酶活性的中和。

获取原文
           

摘要

Herpes simplex virus type 1 ribonucleotide reductase is associated with two polypeptides of apparent molecular weights 136,000 and 38,000. The two polypeptides form a tight complex and, therefore, are often coprecipitated by monoclonal antibodies. We report here that immunoglobulins G purified from polyclonal rabbit antisera (P9) raised against a nonapeptide corresponding to the carboxy terminus of the 38,000-dalton polypeptide specifically neutralize the herpes simplex virus ribonucleotide reductase activity. We suggest that the P9 immunoglobulin G neutralizes the reductase activity by impairing the association of the two subunits (H1 and H2) of the enzyme.
机译:单纯疱疹病毒类型1核糖核苷酸还原酶与表观分子量136,000和38,000的两种多肽有关。两种多肽形成紧密复合物,因此通常通过单克隆抗体共沉淀。在此报告,从多克隆兔抗血清(P9)纯化的免疫球蛋白G升高对应于38,000-dalton多肽的羧基末端的非肽,特别是中和疱疹病毒核糖核糖核苷酸还原酶活性。我们表明P9免疫球蛋白G通过损害酶的两个亚基(H1和H2)的关联来中和还原酶活性。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号