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篇名
綠膿桿菌色氯酸合成酶的活性及調節研究
並列篇名
Studies on tryptophan synthetase enzyme activity and its regulation in Pseudomonas aeruginosa
作者 蔡碧嬋 (Bih-Charn Tsai)劉蔡珊珊 (San-San Tsay Liu)
英文摘要
Tryptophan synthetase of Pseudomonas aeruginosa has a different optimum pH value in different buffer systems. In the phosphate buffer system, the optimum pH value was 7.4 and in tris, 7.9. The maximum reaction velocity was higher in phosphate buffer than in tris. The reaction velocity was found to be proportional to incubation time over a period of twenty minutes, and to the protein concentration in a range of 0 to 600 µg per tube, The enzyme can carry on the reaction at a very low concentration of coenzyme pyridoxal phosphate (1×10^-3 M). The Km for serine was 2.0×10^-3 M and that for indole was 1.25×10^-3 M. The concentration of serine (3.7×10^-2 M) used in experiment had reachted the saturation point while that of indole (2.5×10^-6 M) had not. The enzyme level of tryptophan synthetase was repressed by the addition of tryptopham, indole and anthranilate, At the same concentration (20 µg/ml ), indole and anthranilate had a greater repression effect on tryptophan synthetase than tryptophan did. The four analogues used in the experiment, 5-methyl tryptophan, 6-methyl tryptophan, indolepropionic acid and indoleacrylic acid, did not have any apparent effect on the growth of Pseudomonas aeruginosa. However, they showed repression on the enzyme level of tryptophan synthetase when they were added to the growth medium.
起訖頁 123-131
刊名 TAIWANIA  
期數 197505 (20:2期)
出版單位 臺灣大學生命科學院;台灣生物多樣性協會
該期刊-上一篇 臺灣菝葜屬的兩新種
該期刊-下一篇 馬鈴薯β澱粉酵素之部分純化與性質
 

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