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- W1992817635 abstract "Abstract β-Galactosidase (EC 3.21.23) was isolated from Escherichia coli grown on 0.01 M selenate and compared with the enzyme from cells grown on sulfate. Neutron activation analyses indicated that only the β-galactosidase from selenate cells contained selenium. Amino acid analyses showed that about 80 of the 150 methionine residues had been substituted by selenomethionine while none of the cystine residues were replaced. The catalytic parameters, Km and vmax, were not changed; however, the stability of the selenium β-galactosidase to heat and urea was decreased. It was noted that the urea-denatured enzyme containing selenium, renatured more rapidly and to a greater extent than did the enzyme with the normal sulfur content. A protein sedimenting with a sedimentation coefficient of 4 S was present during most of the isolation steps of both sulfur and selenium enzymes. The relative amount present in the selenium preparation was, however, much greater. Amino acid analysis suggested that this 4-S protein may be a subunit of the active β-galactosidase. A greater number of the methionines of the selenium 4-S protein were replaced by selenomethionine than in the active enzyme. The cystine contents were, however, nearly the same in both preparations." @default.
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- W1992817635 date "1967-08-01" @default.
- W1992817635 modified "2023-10-03" @default.
- W1992817635 title "The isolation and properties of β-galactosidase from Escherichia coli grown on sodium selenate" @default.
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- W1992817635 doi "https://doi.org/10.1016/0304-4165(67)90187-0" @default.
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