Ref ID : 7326
Ono Kouki, Okihashi Masahiro, Inui Hiroshi, Miyatake Kazutaka, Kitaoka Shozaburo, and Nakano Yoshihisa; Purification and Characterization of Isocitrate Lyase from Ethanol-grown Euglena gracilis. J.Eukaryot.Microbiol. 41(6):536-539, 1994
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Isocitrate lyase was purified to homogeneity from ethanol-grown Euglena gracilis. The specific activity was 0.26 µmol/min/mg protein. The molecular mass of the enzyme was calculated to be 380 kDa by gel filtration on a Superose 6 column. The subunit molecular mass of the enzyme was 116 kDa as determined by SDS-polyacrylamide gell electrophoresis. These results showed that the native form of this enzyme was a trimer composed of three identical subunits. The pH optimum for cleavage and condensation reactions was 6.5 and 7.0, respectively. The Km values for isocitrate, glyoxylate and succinate were 3.8, 1.3 and 7.7 mM, respectively. Isocitrate lyase absolutely required Mg2+ for enzymatic activity. This is the first report of the purification of isocitrate lyase to homogeneity from Euglena gracilis.