Unit

UNIT 4.34 Purification of Arsenic (+3 Oxidation State) Methyltransferase from Rat Liver Cytosol

  1. Zuzana Drobna1,
  2. Miroslav Styblo1,2,
  3. David J. Thomas3

Published Online: 1 NOV 2009

DOI: 10.1002/0471140856.tx0434s42

Current Protocols in Toxicology

Current Protocols in Toxicology

How to Cite

Drobna, Z., Styblo, M. and Thomas, D. J. 2009. Purification of Arsenic (+3 Oxidation State) Methyltransferase from Rat Liver Cytosol. Current Protocols in Toxicology. 42:4.34:4.34.1–4.34.13.

Author Information

  1. 1

    Department of Nutrition, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina

  2. 2

    Center for Environmental Medicine, Asthma, and Lung Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina

  3. 3

    Pharmacokinetics Branch, Experimental Toxicology Division, National Health and Environmental Effects Research Laboratory, Office of Research and Development, U.S. Environmental Protection Agency, Research Triangle Park, North Carolina

Publication History

  1. Published Online: 1 NOV 2009
  2. Published Print: NOV 2009

Abstract

Demonstrating the enzymatic basis of arsenic methylation is critical to further studies of the pathway for the conversion of inorganic arsenic into a variety of methylated metabolites. This protocol describes a procedure for the purification of an arsenic methyltransferase from rat liver cytosol. Purification of this enzyme and subsequent cloning of its gene has permitted studies of enzyme structure and function, and has lead to the identification of orthologous genes in genomes of organisms ranging in complexity from sea urchins to humans. These proteins are referred to as arsenic (+3 oxidation state) methyltransferases. Curr. Protoc. Toxicol. 42:4.34.1-4.34.13. © 2009 by John Wiley & Sons, Inc.

Keywords:

  • arsenic;
  • methylation;
  • methyltransferases;
  • protein purification;
  • chromatofocusing;
  • affinity chromatography