Properties of Isocitrate Lyase from an Alkane-utilizable Yeast, Candida tropicalis
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概要
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Isocitrate lyase (EC 4.1.3.1) was purified from the peroxisome-containing particulate fraction of an alkane-grown yeast, Candida tropicalis, which had a conspicuous number of peroxisomes. The properties of the isocitrate lyase, which was induced by alkanes and localized in peroxisomes, were compared with those of the constitutive enzyme purified from glucose-grown cells of the yeast, which contained only a few pre-existing peroxisomes. The molecular masses of both enzymes were estimated to be about 130, 000 daltons by gel-filtration chromatography, and they were both composed of two identical subunits of a molecular mass of 65, 000 daltons. Both enzymes showed similar peptide maps upon partial digestion with proteolytic enzymes and were indistinguishable immunochemically, although there was a slight difference in their amino acid compositions.
- 社団法人 日本農芸化学会の論文
著者
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Uchida Masaaki
Laboratory Of Industrial Biochemistry Department Of Industrial Chemistry Faculty Of Engineering Kyot
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Fukui Saburo
Laboratory Of Industrial Biochemisryt Department Of Industrial Chemistry Faculty Of Engineering Kyot
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OKADA Hirofumi
Laboratory of Industrial Biochemistry, Department of Industrial Chemistry, Faculty of Engineering, K
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Tanaka Atsuo
Laboratory Of Applied Biological Chemistry Department Of Synthetic Chemistry And Biological Chamistr
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Ueda Mitsuyoshi
Laboratory Of Applied Biological Chemistry Department Of Synthetic Chemistry And Biological Chemistr
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MATSUKI Toshitsugu
Laboratory of Industrial Biochemistry, Department of Industrial Chemistry, Faculty of Engineering, Kyoto University
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