Immobilization of Recombinant Firefly Luciferase. Physicochemical Properties and Application

I. A. Lundovskikh, E. I. Dementieva^*, and N. N. Ugarova

School of Chemistry, Lomonosov Moscow State University, Moscow, 119899 Russia; fax: (095) 939-5417; E-mail: unn@enzyme.chem.msu.su

^* To whom correspondence should be addressed.

Received October 17, 1997

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Immobilization of the recombinant Luciola mingrelica and Photinus pyralis firefly luciferases on BrCN-activated Sepharose was investigated. The catalytic properties and analytical characteristics of the immobilized recombinant and native luciferases were comparatively studied. The catalytic properties of the immobilized recombinant L. mingrelica luciferase are close to those of the native luciferase, but the former enzyme appeared to be significantly more stable. The immobilized recombinant luciferases can be used for ATP assay within the 0.01-10000 nM range.

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KEY WORDS: recombinant firefly luciferase, immobilization, BrCN-activated Sepharose, ATP assay

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