Luciferases


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Luciferases

 

enzymes that participate in bioluminescence.

Luciferases catalyze the aerobic oxidation of luciferins, the result of which is the conversion of the substrate to the electron-excited state and the release of the excess energy as light quanta. Living organisms store luciferases in photogenic cells or in specialized luminescence organs. Flavoprotein (molecular weight [mol wt], 85,000) is the luciferase in species of Achromobacter. Crayfish of the genus Cypridina contain an albumin (mol wt, 37,000-45,000), and beetles of the genus Photinus contain the luciferase euglobulin (approximate mol wt, 100,000). Even in organisms that contain the same luciferase, such as all species of fireflies, there are differences in luciferase structure and in the optimum conditions for its activity.

References in periodicals archive ?
After 24 hours, the medium was aspirated with Thermo Scientific Versette Automated Liquid Handler, and luciferase activity was measured in each well with the Dual Luciferase Assay Reporter System (Promega).
Researchers are now able to easily insert luciferase genes into the cells of interest, administer them to animal models, and immediately identify not only the organs that they populate but also their viability, proliferation, and any changes in biodistribution that might occur over time.
Red-emitting luciferases for bioluminescence reporter and imaging applications.
Many proteins are used as reporter proteins , for example chloramphenicol acetyltransferase (CAT) , [beta] galactosidase and luciferase. Firefly luciferases are abundantly utilized as gene reporter and catalyze a bioluminescense reaction which are directly detected.
These creatures all owe their glow to an enzyme called luciferase.
These cells contain luminous materials: luciferin and either luciferase or a luciferin-binding photoprotein.
In addition, the expressed enzyme and the gene for the bioluminescent luciferase class of enzymes have considerable potential as labels for nucleic acid assays.
"A real revolution has come from our ability to look at how genes work," says Wood, who first basked in the glow of scientific luminosity in 1986 when he and co-workers made the world's first glow-in-the-dark tobacco plants by splicing into the plants a luciferase gene from a firefly.
The molecular weights of luciferases A, B, and C were estimated by gel filtration on the same Superdex 200 Prep column that was used in Step 6 to purify the luciferases; 0.005% LCC was added to the buffer to minimize adsorption onto the column.
Significance of the existence of two different luciferases
Friedrich and Greenberg [38] reported that growth on carbon source other than glycerol such as glucose elicited catabolite repression of luciferase activity, hence the lag phase observed.