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- W1937305668 abstract "A cDNA containing the complete coding sequence for rat liver S-adenosylmethionine synthetase was cloned into the prokaryotic expression vector pT7-7 and expressed in Escherichia coli BL21(DE3). A major additional band corresponding to a protein of 48 kDa was detected on SDS/PAGE after induction with isopropyl beta-D-thiogalactopyranoside. This protein was distributed in both the soluble and insoluble fractions and accounted for approx. 30% of the total bacterial protein. The soluble enzyme was fully active, as revealed by assays in vitro of S-adenosylmethionine synthetase activity. In addition, transformed bacteria exhibited highly increased levels of intracellular S-adenosylmethionine. Two active forms of the recombinant enzyme, with apparent molecular masses of 210 kDa and 110 kDa, were detected when cytosolic extracts of the transformed cells were fractionated by gel-filtration chromatography. It is concluded that the expressed S-adenosylmethionine synthetase polypeptide assemble as tetramers and dimers." @default.
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- W1937305668 date "1994-07-15" @default.
- W1937305668 modified "2023-10-17" @default.
- W1937305668 title "Expression of rat liver <i>S</i>-adenosylmethionine synthetase in <i>Escherichia coli</i> results in two active oligomeric forms" @default.
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- W1937305668 doi "https://doi.org/10.1042/bj3010557" @default.
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