Expression of rat liver S-adenosylmethionine synthetase in Escherichia coli results in two active oligomeric forms.

@article{Alvarez1994ExpressionOR,
  title={Expression of rat liver S-adenosylmethionine synthetase in Escherichia coli results in two active oligomeric forms.},
  author={Luc{\'i}a P{\'e}rez Alvarez and Jes{\'u}s Mingorance and Mar{\'i}a Angeles Pajares and Jose M. Mato},
  journal={The Biochemical journal},
  year={1994},
  volume={301 ( Pt 2)},
  pages={557-61}
}
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… CONTINUE READING
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