93(P-2) ラチア生物発光の分子基盤(ポスター発表の部)

概要

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(1) Purification of Latia luciferase was achieved by a 5-step procedure including affinity chromatography on a Con A-supported column. (2) The purified luciferase exhibited a luciferin/luciferase reaction with Latia luciferin (1) without any cofactors such as "purple protein," and gave the same bioluminescence spectrum as those obtained with the crude luciferase containing "purple protein," indicating that the light emitter of Latia bioluminescence is a fluorophore present in the luciferase molecule. (3) The bioluminescent-active luciferase was found to have a molecular mass of 150kDa and to be present as an oligomer of bioluminescent-inactive monomers having a molecular mass of 31kDa. (4) The Latia luciferase was found to be a glycoprotein. The glycoside moiety may be important for keeping the oligomeric structure and/or for bioluminescence reaction. (5) Studies on substrate specificity using a series of luciferin analogs suggested that the Latia luciferase recognized strictly the 2,6,6-trimethylcyclohexene ring moiety in the luciferin structure. The enol acetate analogue (E-6) possessed 60% activity compared to natural luciferin (1) with an enol formate structure, indicating the formate moiety to be not essential for the Latia bioluminescence reaction.
天然有機化合物討論会の論文
2000-10-01