Bacterial luciferase purification

Gunsalus-Miguel, A., et al. (1972). Purification and properties of bacterial luciferases. J. Biol. Chem. 247 398-404. 

Lang, D., Erdmann, H., and Schmid, R. D. (1992). Bacterial luciferase of Vibrio harveyi MAV purification, characterization and crystallization. Enzyme Microb. Technol. 14 479-485. 

Bacterial bioluminescence, 30-46 factors required, 31 general scheme, 32 in vivo luminescence, 41 luminescence reaction, 37, 38 Bacterial luciferase, 33-35, 343 assay, 39 cloning, 34 crystal structure, 34 extraction and purification, 34 inactivation, 34, 35 molecular weight, 34 properties, 34 storage, 35 subunits, 34... 

Hastings J.W., Baldwin T.O., Nicoli M.Z., Bacterial luciferase assay, purification and properties, Methods Enzymol. 1978 57 135-152. 

The technique of gel filtration in mixed solvents at subzero temperatures was first used to purify unstable oxygenated compounds of bacterial cytochrome P-450 from the reducing products used in their preparation. The second application concerns the purification of transient oxygenated compounds of bacterial luciferase. 

Tyulkova N. Purification of bacterial luciferase from Photobacterium leiognathi with use FPLS-system. In Jezowska-Trzebiatowska B. ed. Biological luminescence. Singapore World Scientific, 1989 369 -74. 

Bacterial luciferase can be purified by various conventional chromatographic techniques (6) and by using a series of HPLC columns (7). One of the new purification techniques relies on an affinity matrix composed of a luciferase inhibitor, 2,2-diphenylpropylamine, conjugated to Sepharose (13,35). The affinity chromatography procedure is reported to give a routine yield (60%) of 600—700 mg of over 90% pure luciferase from a 500 g batch of cell paste. 

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