Characterization of amine oxidase activities in macrophages from human peripheral blood.
A sensitive assay for the determination of hydrogen peroxide formation and a method for the identification and characterization of amine oxidases in cells and other oxidase sources of limited accessibility are described. The enzymes are characterized by substrate and inhibitor patterns. The method was applied to the identification and characterization of polyamine oxidizing enzymes in macrophages from human peripheral blood. The major oxidase activity in these cells was found to be a tissue-type polyamine oxidase, but with distinct characteristics. Diamine oxidase and monoamine oxidase activities were also detected in homogenates of macrophages. Since the formation of toxic products by a releasable polyamine oxidase is supposed to be an integral part of a regulatory function of macrophages, we consider our work as a basis for the elucidation of this function.
Seiler
N
N
URA CNRS 1529-DRED 1266, Laboratoire de biologie cellulaire, Université 1, Faculté de médecine, Rennes, France.
Moulinoux
J P
JP
Havouis
R
R
Toujas
L
L
D006631:Amine Oxidase (Copper-Containing); D002478:Cells, Cultured; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism; D008264:Macrophages / Q000201:enzymology*; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000032:analysis*; D013379:Substrate Specificity
D006861:Hydrogen Peroxide; D006631:Amine Oxidase (Copper-Containing); D000587:Oxidoreductases Acting on CH-NH Group Donors