Summary.
Handling and detoxification of metals by enzymes is a major issue that is not in the focus of current biomedical research concepts. The finding of the presence of arsenic (+3 Oxidation State) methyltransferase (AS3MT) in neuroblastoma cells NE-115 as a high abundance protein made us investigate primary structure of AS3MT reflecting an example of metal-handling in eucaryotes. Proteins extracted from NE-115 cells were run on 2-DE followed by two different mass spectrometrical methods. High sequence coverage was obtained by multiple protease digestion and a sequence conflict was solved at arginine 335.
These findings are important when future studies on this enzyme are designed at the protein level and in particular, when antibodies against this protein will be generated.
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Authors’ address: Prof. Gert Lubec, Department of Pediatrics, Medical University of Vienna, Währinger Gürtel 18, A-1090 Vienna, Austria
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John, J., Oh, JE., Pollak, A. et al. Identification and characterisation of arsenite (+3 Oxidation State) methyltransferase (AS3MT) in mouse neuroblastoma cell line N1E-115. Amino Acids 35, 355–358 (2008). https://doi.org/10.1007/s00726-007-0613-1
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DOI: https://doi.org/10.1007/s00726-007-0613-1