Absence of plasma amine oxidase in some frequently used animal models

• Published in: Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology Vol. 106; no. 2; pp. 483 - 487
• Main Authors: Ebong, Samuel, Farkas, Walter R.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Inc 01.10.1993; Pergamon
• Subjects: Amine Oxidase (Copper-Containing); Ammonia - metabolism; Analytical, structural and metabolic biochemistry; Animals; Benzylamines - metabolism; Biological and medical sciences; Cats; Cattle; Chromatography, Paper; Cricetinae; Dogs; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Guinea Pigs; Horses; Humans; Mice; Models, Biological; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on CH-NH Group Donors - blood; Rabbits; Rats; Species Specificity; Substrate Specificity; Swine; Animal model; Vertebrata; Mammalia; Enzymatic activity; Enzyme; Substrate specificity; Species specificity; Oxidoreductases; Localization; Amine oxidase (copper-containing)
• ISSN: 0742-8413
• DOI: 10.1016/0742-8413(93)90167-J

1. Plasma amine oxidase (PAO), an enzyme that oxidizes primary amines is generally assumed to be present in the sera of all mammals. 2. We studied plasma from eleven different mammals to determine if they could oxidize a group of amines of biomedical interests. 3. Our results indicate that PAO is not present in all mammals and also that substrate specificity of the enzyme varies within the species tested. Rodents which are frequently used as animal models in pharmacology and toxicology do not contain PAO. 4. The common polyamines, spermine, spermidine and putrecine were oxidized only by bovine plasma.