Naunyn-Schmiedeberg's Archives of Pharmacology

, Volume 313, Issue 3, pp 263–268

Studies on lung N-methyltransferases, a pharmacological approach

  • Robert G. Pendleton
  • George Gessner
  • John Sawyer
Article

DOI: 10.1007/BF00505743

Cite this article as:
Pendleton, R.G., Gessner, G. & Sawyer, J. Naunyn-Schmiedeberg's Arch. Pharmacol. (1980) 313: 263. doi:10.1007/BF00505743

Summary

Phenylethanolamine N-methyltransferase (PNMT) was identified as the primary, high affinity N-methylating enzyme for phenylethanolamine (PEA) in rat, dog and Rhesus monkey lung. Human and rabbit lung, however, do not contain this enzyme but possess a more non-specific or general N-methyltransferase with a relatively low affinity for PEA and for which β-phenethylamine (β-PE) is also a substrate. The former but not the latter enzyme is markedly inhibited by micromolar concentrations of the PNMT antagonist, SK & F 64139. This evidence indicates that certain species differences exist for the enzyme system(s) available for the N-methylation of phenethylamine-type compounds in pulmonary tissue.

Key words

PNMT SK&F 64139 Lung enzymes 

Copyright information

© Springer-Verlag 1980

Authors and Affiliations

  • Robert G. Pendleton
    • 1
  • George Gessner
    • 1
  • John Sawyer
    • 1
  1. 1.Smith Kline and French LaboratoriesPhiladelphiaUSA

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