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KMID : 1024519980070060853
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Journal of the Environmental Sciences
1998 Volume.7 No. 6 p.853 ~ p.857
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Purification of Isocitrate lyase Produced from Microbacterium laevaniformans
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Suh Seung-Kyo
Kim Jung-Ho
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Abstract
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Purification of the isocitrate lyase extracted from Microbacterium laevaniformans was investigated. The isocitrate lyase was purified 43.6 folds by the following continuous treatment with ammonium sulfate fraction, DEAE-cellulose, DEAE-sephacel and Sephadex G-200 chromatography. The purified isocitrate lyase was showed to be a single protein band by polyacrylamide gel electrophoresis. The molecular weight of the purified isocitrate lyase was estimated 54,000 Da by the SDS-polyacrylamide gel electrophoresis. The Km and Vmax values for isocitrate were estimated to be 0.83mM and 0.33units/ml, respectively. Activity of isocitrate lyase was inhibited by cystein-HCl and glutathione.
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KEYWORD
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Purification, Isocitrate lyase, Microbacterium laevaniformans
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