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  • 标题:Immobilization of bacterial luciferase and FMN reductase on glass rods
  • 本地全文:下载
  • 作者:E Jablonski ; M DeLuca
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1976
  • 卷号:73
  • 期号:11
  • 页码:3848-3851
  • DOI:10.1073/pnas.73.11.3848
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Bacterial luciferase and NAD(P)H: FMN oxidoreductase isolated from Beneckea harveyi were covalently linked via diazotization to arylamine porous glass beads which had been cemented onto plain glass rods. These immobilized enzymes are individually active and also function to produce light via a coupled reaction utilizing NADH or NADPH. These enzymes have properties similar to the soluble forms with regard to pH and substrate optima and also exhibit linearity in peak intensity of the initial flash of light emitted as a function of NADH or NADPH concentration. Linearity with NADH is obtained in the range of 1 pmol to 50 nmol, and between 10 pmol to 200 nmol for NADPH. The bound enzymes are stable and reusable. This immobilized system offers a rapid and inexpensive m
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