Methylenetetrahydrofolate reductase. Evidence for spatially distinct subunit domains obtained by scanning transmission electron microscopy and limited proteolysis.

@article{Matthews1984MethylenetetrahydrofolateRE,
  title={Methylenetetrahydrofolate reductase. Evidence for spatially distinct subunit domains obtained by scanning transmission electron microscopy and limited proteolysis.},
  author={Rowena G. Matthews and Maria Antonietta Vanoni and James F. Hainfeld and J Wall},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 19},
  pages={11647-50}
}
Scanning transmission electron microscopy of individual unfixed molecules of methylenetetrahydrofolate reductase has been used to determine the molecular mass distribution of the protein. Methylenetetrahydrofolate reductase, which has a subunit molecular mass of 77 kilodaltons, was found to exist predominantly as a dimer with an apparent molecular mass of 136 +/- 29 kilodaltons. The mass distribution of the enzyme molecules was unchanged in the presence of the allosteric inhibitor S… CONTINUE READING

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