Abstract
Isocitrate lyase has been purified to homogeneity, as determined by SDS-polyacrylamide gel electrophoresis and subsequent silver staining, fromEscherichia coli D5H3G7. The enzyme was found to have a subunit molecular weight of 48,000 and a native molecular weight of 188,000 as determined by gel filtration chromatography. Thus, the enzyme appears to have tetrameric structure. The isoelectric point was determined to be 4.6, and the enzyme displayed a pH optimum at 7.3. The Km of isocitrate lyase forthreo-Ds-isocitrate was determined to be 8 μM. The purification procedure is highly reproducible and results in a 39% net yield of purified protein.
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Robertson, E.F., Reeves, H.C. Purification and characterization of isocitrate lyase fromEscherichia coli . Current Microbiology 14, 347–350 (1986). https://doi.org/10.1007/BF01568702
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DOI: https://doi.org/10.1007/BF01568702