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- W1976107003 abstract "A simple procedure is reported for the purification of the two malate synthases of Escherichia coli involved in the use of acetate (A) and glycolate (G), respectively, as carbon source. Both isoenzymes have been isolated simultaneously and in equally high amounts from a strain constitutive for the glyoxylate cycle, after growth on glycolate. After separation from each other by column chromatography on DEAE-cellulose, the malate synthases have been purified by heating, ammonium sulfate precipitation and molecular sieve chromatography on a Sephadex G-200 column, in the constant presence of their specific protectors, glycolate for malate synthase A, and oxalate for malate synthase G. The purified preparations so obtained appeared to be homogeneous on the basis of analytical ultracentrifugation and moving-boundary electrophoresis. The sedimentation coefficient at infinite dilution was 4.6 S for malate synthase A and 5.2 S for malate synthase G; their electrophoretic mobilities at pH 8 were 4.3 X 10−5 cm2 V−1 s−1 and 4.1 × 10−5 cm2 V−1 s−1, respectively. The apparent molecular weight of malate synthase A, estimated by Archibald's method, was 54000; that of malate synthase G, estimated by light scattering, was 52000. Threonine and serine have been found, by Sanger's method, to be N-terminal residues of malate synthases A and G, respectively." @default.
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- W1976107003 date "1973-09-01" @default.
- W1976107003 modified "2023-09-27" @default.
- W1976107003 title "Purification et caracterisation partielle des deux malate synthases d'Escherichia coli" @default.
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- W1976107003 doi "https://doi.org/10.1111/j.1432-1033.1973.tb03001.x" @default.
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