緑葉におけるリボフラビン生合成にかんする研究 : (IV)リボフラビン合成酵素の活性化と安定化

概要

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Riboflavin synthetase which is widely spread in plants and microorganisms catalyzes the formation of riboflavin from 6,7-dimethyl-8-ribityllumazine. In the progress of purification, this enzyme preparation is rapidly inactivated in solution. It was found that the enzyme was activated and stabilized by certain reducing agents such as Na_2S0_3 and dithiothreitol in the present work. Activation of the enzyme by the addition of both Na_2S0_3 (10mM) and dithiothrertol (10mM) for 2hr at 2℃ showed about 53% as compared with the system in which reducing agents were absent. Maximum concentration of Na2S03 and dithiothreitol for the production of riboflavin was 5〜10 mM. The enzyme solution in which Na_2S0_3 (10mM) and dithiothreitol (5mM) were added, was well preserved for ten days at 2℃, while in the absence of reducing agents, this activity was lost by half times and it was impossible to regain the lost activity by adding Na_2S0_3 and dithiothreitol before the reaction-start.
日本ビタミン学会の論文
1969-10-25