Studies on the metabolism of norepinephrine, epinephrine and their o-methyl analogs by partially purified enzyme preparations

https://doi.org/10.1016/0003-9861(58)90089-4Get rights and content

Abstract

Studies concerning the actions of a soluble, partially purified monoamine oxidase (MAO) on norepinephrine and other catecholamines and on their 3-methoxy analogs are presented. The intermediate in the oxidation of norepinephrine to 3, 4-dihydroxymandelic acid has been shown to be 3, 4-dihydroxyphenylglycolic aldehyde, and some properties of the latter compound are presented. The roles of MAO and catechol-O-methylpherase in the in vivo metabolism of norepinephrine and epinephrine are discussed.

References (15)

  • R.W. Schayer

    J. Biol. Chem

    (1951)
  • R.W. Schayer et al.

    J. Biol. Chem

    (1952)
  • M.D. Armstrong et al.

    Biochim. et Biophys. Acta

    (1957)
  • H. Weissbach et al.

    J. Biol. Chem

    (1957)
  • H. Kalckar

    J. Biol. Chem

    (1947)
  • G.H. Hogeboom et al.

    J. Biol. Chem

    (1948)
  • H.D. Gibbs

    J. Biol. Chem

    (1927)
There are more references available in the full text version of this article.

Cited by (0)

A preliminary report of this work was presented to the American Society for Pharmacology and Experimental Therapeutics in Baltimore, September, 1957.

2

Part of this work will be presented in a thesis by Lemuel C. Leeper in partial fulfillment of the requirements for the degree of Doctor of Philosophy, Department of Chemistry, Georgetown University, Washington, D. C.

View full text