Abstract
Semicarbazide-sensitive amine oxidases with a high affinity for benzylamine (Bz.SSAO) (E.C.1.4.3.6) have been biochemically described in many mammalian tissues (adipose tissue, lung, heart, blood vessels). The enzymic activity appears to be expressed by mesenchymal cells (fibroblasts, adipocytes, smooth muscles). Although the physiological role of this enzymic activity is still unclear, some possible physiological substrates such as histamine are discussed. Some enzymes of this class (SSAO) have been purified. They share many similarities, among which are that they contain copper and a carbonyl active site. The nature of the organic cofactor of these enzymes is discussed and data are presented which have identified pyridoxal in pig kidney diamine oxidase and in pig plasma benzylamine oxidase by gas chromatography-mass spectrometry.
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