PARTIAL PURIFICATION AND PROPERTIES OF BACTERIAL LUCIFERIN AND LUCIFERASE

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Abstract
The light-emitting system was separated from the luminous bacterium, Achromobacter fischeri. By acid precipitation and (NH4)2SO4 fractionation the enzyme was purified approx. 10 times. With the partially purified enzyme it is possible to show for light emission an absolute requirement for reduced diphos-phopyridine nucleotide and flavin adenine dinucleotide. A 3d unknown component is essential for light emission. This factor, tentatively classified as bacterial luciferin, can be obtained from a var. of sources including, in addition to bacteria, mouse liver and spleen. It is necessary to irradiate with near u.-v. light (Keese lamp) before extracts from these sources are active. The luminescent reaction is sensitive to cyanide, versene and particularly riboflavin. The effect of cyanide is reduced by adding additional luciferin to the reaction. The results suggest the possibility of a metal involvement in bacterial luminescence. The results are discussed and compared to luminous reactions extracted from other organisms.

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