Behaviour and properties of catechol-O-methyltransferase from human placenta

  • K. F. Tipton
  • N. Nic a’ Bháird
Conference paper
Part of the Journal of Neural Transmission book series (NEURAL SUPPL, volume 32)


A procedure is reported for the purification of human placental catechol-O-methyltransferase. The preparation is apparently homogeneous and behaves as a monomer with an approximate Mr of 23,000. The sequence of the first 21 amino acid residues from the N-terminal end of the protein is reported. The activity of the enzyme is strongly influenced by the nature of the buffer in which it is assayed.


Potassium Phosphate Buffer Ammonium Sulphate Buffer Concentration Relative Molecular Mass Potassium Acetate 
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Copyright information

© Springer-Verlag 1990

Authors and Affiliations

  • K. F. Tipton
    • 1
  • N. Nic a’ Bháird
    • 1
  1. 1.Department of BiochemistryTrinity CollegeDublin 2Ireland

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