Sequence-specific BamHI methylase. Purification and characterization.

@article{Nardone1984SequencespecificBM,
  title={Sequence-specific BamHI methylase. Purification and characterization.},
  author={Glenn A. Nardone and J George and J. G. Chirikjian},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 16},
  pages={
          10357-62
        }
}
BamHI methylase has been purified to apparent homogeneity. The isolated form of the enzyme is a single polypeptide with a molecular weight of 56,000 as determined by sodium dodecyl sulfate-polyacrylamide electrophoresis. Unlike BamHI endonuclease, which is isolated as a dimer and higher aggregates, the methylase has no apparent higher form. The methylase requires S-adenosyl-L-methionine as the methyl-group donor and is inhibited by Mg2+. The enzyme is also inhibited by 2,3-butanedione and… Expand
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