A streptavidin-luciferase fusion proteins: Comparisons and applications

Matti Karp (Corresponding Author), Christian Oker-Blom

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Luciferases are unique enzymes in being capable of emitting visible light as one of the end-products of their catalysis. Both procaryotic and eucaryotic organisms exist that emit light, and the luciferases from these organisms differ considerably in size as well as chemistry of catalysis. Two main, i.e. most studied groups, are the bacterial luciferases of e.g. Vibrio fisheri, Vibrio harveyi, and Photorhabdus luminescens, responding to FMNH2, long-chain aldehyde and molecular oxygen and the insect luciferases of the fireflies Photinus pyralis and Luciola minengrelica or click beetle Pyrophorus plagiophthalamus, responding to ATP, luciferin and molecular oxygen. An emerging amount of ‘new’ luciferases from shrimps, fish, jelly fish and overall from marine origin, are finding their way to biotechnological applications. The common feature of these is their ability to produce light within the visible region of the spectrum, i.e. between 450 nm (blue) and 630 nm (red). In this short review, we discuss some of the recent advances on fusion proteins of eucaryotic luciferases and their applications. Special emphasis is placed on a streptavidin–luciferase fusion protein produced by insect cells using the baculovirus expression system.
Original languageEnglish
Pages (from-to)101-104
JournalBiomolecular Engineering
Volume16
Issue number1-4
DOIs
Publication statusPublished - 1999
MoE publication typeA1 Journal article-refereed

    Fingerprint

Cite this