Purification and properties of isocitrate lyase from pupas of the butterfly Papilio machaon L.
作者： A. T. Eprintsev , M. Yu. Shevchenko , V. N. Popov
DOI: 10.1023/B:BIRY.0000026191.66573.AA
关键词: Enzyme 、 Biology 、 Size-exclusion chromatography 、 Isocitrate lyase 、 Glyoxylate cycle 、 Papilio machaon 、 Malate synthase 、 Specific activity 、 Biochemistry 、 Protein subunit
摘要: Key enzymes of the glyoxylate cycle, isocitrate lyase and malate synthase, were identified in pupas butterfly Papilio machaon L. The activities these 0.056 0.108 unit per mg protein, respectively. Isocitrate was purified by a combination various chromatographic steps including ammonium sulfate fractionation, ionexchange chromatography on DEAE-Toyopearl, gel filtration. specific activity enzyme 5.5 units which corresponded to 98-fold purification 6% yield. followed Michaelis–Menten kinetics (Km for isocitrate, 1.4 mM) competitively inhibited succinate (Ki = 1.8 1 mM). study physicochemical properties showed that it is homodimer with subunit molecular weight 68 ± 2 kD pH optimum 7.5 (in Tris-HCl buffer).
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