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김택영,위세찬 ( Taik Young Kim,Se Chan Wee 생화학분자생물학회 1975 BMB Reports Vol.8 No.3
Isocitrate lyase and malate synthetase were found to be active in Brevibacterium anamoniagenes grown on the acetate media, indicating that the glyoxylate cycle was operated. The specific activity of the isocitrate lyase from the acetate media showed about 70 times greater than that from the glucose media. The optimum pH for the partially purified isocitrate lyase was 7.0∼7.2 and Km value for the DL-isocitrate was determined as 0.41 mM. The effects of divalent ions were studied. Magnesium ion was an effective activator, but calcium, cobalt, cupric, ferrous, and manganese ions were found to precipitate in the assay mixtures. Iodoacetate, p-hydroxymercuribenzoate and phosphoenolpyruvate were the strong inhibitors for the enzyme. Phosphoenolpyruvate inhibited the enzyme to 78% at pH 6.85 and 47% at pH 7.25. A possible mechanism of the phosphoenolpyruvate to the regulation of the glyoxylate cycle was discussed.