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  • Title: Purification and properties of diamine oxidase from Euphorbia latex.
    Author: Rinaldi A, Floris G, Finazzi-Agro A.
    Journal: Eur J Biochem; 1982 Oct; 127(2):417-22. PubMed ID: 6814913.
    Abstract:
    A diamine oxidase has been purified to homogeneity from the latex of an herbaceous shrub, Euphorbia characias. This enzyme has a relative molecular mass of 144,000 and is composed of two identical subunits. It contain two Cu(II) and two carbonyl-like groups per dimer. The purified enzyme is pink and shows a broad absorption in the visible region centered at 480 nm, which is modified by the addition of phenylhydrazine or semicarbazide. The electron paramagnetic resonance spectrum is typical of copper(II) in a tetragonal symmetry. This enzyme oxidizes putrescine and cadaverine at fairly high rate and, less efficiently a few related compounds, but not histamine, spermine or spermidine.
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