细菌荧光素酶和FMN还原酶在玻璃棒上的固定化。
Immobilization of bacterial luciferase and FMN reductase on glass rods.
作者信息
Jablonski E, DeLuca M
出版信息
Proc Natl Acad Sci U S A. 1976 Nov;73(11):3848-51. doi: 10.1073/pnas.73.11.3848.
Abstract
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
摘要
从哈维贝内克氏菌中分离出的细菌荧光素酶和NAD(P)H：FMN氧化还原酶，通过重氮化反应与固定在普通玻璃棒上的芳胺多孔玻璃珠共价连接。这些固定化酶各自具有活性，并且还能通过利用NADH或NADPH的偶联反应产生光。这些酶在pH值和底物最佳条件方面具有与可溶性形式相似的特性，并且在作为NADH或NADPH浓度函数发出的初始闪光的峰值强度方面也表现出线性关系。与NADH的线性关系在1皮摩尔至50纳摩尔范围内获得，与NADPH的线性关系在10皮摩尔至200纳摩尔之间。结合的酶稳定且可重复使用。这种固定化系统提供了一种快速且廉价的…… （原文最后单词不完整）
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