Association of diamine oxidase with microsomal membranes in rabbit liver

Diamine oxidase (diamine O 2 oxidoreductase, EC 1.4.3.6, DAO) of rabbit liver is localized in the microsomal fraction (1, 2). Microsomes, freed of adsorbed and intraluminal proteins by washing procedures, still retain all DAO activity. This indicates that DAO belongs to the microsomal membrane itsel...

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Veröffentlicht in:	Life sciences (1973) 1974-12, Vol.15 (11), p.1909-1915
Hauptverfasser:	Argento Cerù, Maria Paola, Sartori, Claudia, Autuori, Francesco
Format:	Artikel
Sprache:	eng
Schlagworte:	Amine Oxidase (Copper-Containing) - analysis Amine Oxidase (Copper-Containing) - metabolism Animals Cadaverine - metabolism Deoxycholic Acid - pharmacology Dose-Response Relationship, Drug Histamine - metabolism Intracellular Membranes - analysis Intracellular Membranes - enzymology Male Membrane Proteins - analysis Microscopy, Electron Microsomes, Liver - analysis Microsomes, Liver - enzymology Microsomes, Liver - ultrastructure Phospholipids - analysis Protein Binding - drug effects Proteins - analysis Rabbits
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Zusammenfassung:	Diamine oxidase (diamine O 2 oxidoreductase, EC 1.4.3.6, DAO) of rabbit liver is localized in the microsomal fraction (1, 2). Microsomes, freed of adsorbed and intraluminal proteins by washing procedures, still retain all DAO activity. This indicates that DAO belongs to the microsomal membrane itself. While the release of DAO activity from washed microsomes occurs exclusively in the presence of high concentrations of deoxycholate, tight binding of this enzyme to the membrane structure is apparent.
ISSN:	0024-3205 1879-0631
DOI:	10.1016/0024-3205(74)90041-1