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- W25518215 abstract "This chapter discusses the use of coimmobilized multienzyme systems as models for in vivo processes. It describes experiments in which firefly and bacterial luciferases were coimmobilized with other enzymes so that compounds produced on the solid support could be measured directly in the microenvironment using the emission of light. The reactions catalyzed by both the firefly luciferase and the bacterial luciferase are irreversible. Luciferases can be used to measure NADH or adenosine triphosphate (ATP) in the microenvironment and photon emission is not subject to diffusional restrictions. Thermodynamically, the enzymes act to pull the sequence of reactions, thus, making it possible to study processes which are thermodynamically unfavorable. All the experiments reported in the chapter were done with enzymes immobilized onto Sepharose 4B in the presence of bovine serum albumin so the entire bead is essentially covered with protein. While the recovery of active enzymes on the Sepharose is variable, in general, it is possible to obtain 15-80 % active enzyme on the beads." @default.
- W25518215 created "2016-06-24" @default.
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- W25518215 date "1984-01-01" @default.
- W25518215 modified "2023-09-26" @default.
- W25518215 title "Use of Coimmobilized Multienzyme Systems as Models for in Vivo Processes" @default.
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- W25518215 doi "https://doi.org/10.1016/b978-0-12-152824-9.50025-3" @default.
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