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.
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