Properties and uses of immobilized light-emitting enzyme systems from Beneckea harveyi.

Author:

Jablonski E,DeLuca M

Abstract

Abstract Bacterial luciferase and NADH:FMN oxidoreductase have been immobilized onto arylamine glass beads. These immobilized enzymes can detect as little as 0.2 pmol of NADH per assay sample. Glucose-6-phosphate dehydrogenase has been co-immobilized with these enzymes, and with this system it is possible to quantitate 1 pmol of glucose 6-phosphate. By co-immobilizing a fourth enzyme, hexokinase, onto the glass beads, the system can reproducibly detect 20 pmol of glucose per liter. These immobilized enzyme systems are potentially superior to soluble enzymes by being reusable and much more stable. We compared the light-emitting properties of the immobilized enzyme systems with that of an equivalent mixture of the soluble enzymes. The most striking difference was the apparently more efficient conversion of NADH or glucose 6-phosphate to light by the immobilized enzymes. We used hydroxysteroid dehydrogenase in developing a soluble coupled system for the assay of androsterone and testosterone. The lower limit of detection was 100 pmol.

Publisher

Oxford University Press (OUP)

Subject

Biochemistry (medical),Clinical Biochemistry

Cited by 27 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Specific Immobilization ofin VivoBiotinylated Bacterial Luciferase and FMN:NAD(P)H Oxidoreductase;Analytical Biochemistry;1999-05

2. Immobilized Enzymes and Cells in Biochemical Reactions;Immobilized Biosystems;1994

3. References;Progress in Clinical Biochemistry and Medicine;1991

4. Luminescence in Biosensor Design;Biosensors with Fiberoptics;1991

5. Bioluminescent assay for serum adenosine deaminase with immobilized bacterial luciferase;Clinica Chimica Acta;1989-10

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