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Specific immobilization of firefly luciferase through a biotin carboxyl carrier protein domain
C Y Wang1, S Hitz, J D Andrade
1Department of Bioengineering, University of Utah, 2480 MEB, Salt Lake City, Utah, 84112, USA.
Analytical Biochemistry
|March 1, 1997
Abstract:
Firefly luciferase (Photinus pyralis) was fused with a histidine tag and a biotin carboxyl carrier protein (BCCP) domain at its amino terminus. Highly purified recombinant luciferase was obtained by a one-step purification protocol, utilizing immobilized metal affinity chromatography. The novel BCCP-luciferase had properties, stability, and activity similar to those of native luciferase. The biotin molecule on the BCCP domain allowed specific immobilization of BCCP-luciferase on avidin-coated surfaces via the biotin-avidin interaction.