A streptavidin-luciferase fusion protein: comparisons and applications

Citation
M. Karp et C. Oker-blom, A streptavidin-luciferase fusion protein: comparisons and applications, BIOMOL ENG, 16(1-4), 1999, pp. 101-104
Citations number
13
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Molecular Biology & Genetics
Journal title
BIOMOLECULAR ENGINEERING
ISSN journal
1389-0344 → ACNP
Volume
16
Issue
1-4
Year of publication
1999
Pages
101 - 104
Database
ISI
SICI code
1389-0344(199912)16:1-4<101:ASFPCA>2.0.ZU;2-O
Abstract
Luciferases are unique enzymes in being capable of emitting visible light a s one of the end-products of their catalysis. Both procaryotic and eucaryot ic organisms exist that emit light, and the luciferases from these organism s 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 fish eri, Vibrio harveyi, and Photorhabdus luminescens, responding to FMNH2, lon g-chain aldehyde and molecular oxygen and the insect luciferases of the fir eflies Photinus pyralis and Luciola minengrelica or click beetle Pyrophorus plagiophthalamus, responding to ATP, luciferin and molecular oxygen. An em erging amount of 'new' luciferases from shrimps, fish, jelly fish and overa ll from marine origin, are finding their way to biotechnological applicatio ns. The common feature of these is their ability to produce light within th e visible region of the spectrum, i.e. between 450 nm (blue) and 630 nm (re d). 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 c ells using the baculovirus expression system. (C) 1999 Elsevier Science B.V . All rights reserved.