Purification and primary structure of snail metallothionein. Similarity of the N-terminal sequence with histones H4 and H2A.

@article{Dallinger1993PurificationAP,
  title={Purification and primary structure of snail metallothionein. Similarity of the N-terminal sequence with histones H4 and H2A.},
  author={Reinhard Dallinger and Burkhard Berger and Peter E. Hunziker and N E Birchler and Charles R. Hauer and Jeremias H. R. K{\"a}gi},
  journal={European journal of biochemistry},
  year={1993},
  volume={216 3},
  pages={739-46}
}
A cadmium-binding metallothionein has been purified from metal-exposed Roman snails (Helix pomatia) using gel-permeation, ion-exchange and reverse-phase high-performance liquid chromatography. The S-methylated protein was digested with trypsin and the endoproteinases Asp-N, Glu-C and Arg-C. While most of the resulting peptides could be sequenced by Edman degradation, the intact protein, as well as the N-terminal peptide, proved to be blocked. Analysis by mass spectrometry showed that the N… CONTINUE READING
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