Abstract
An amine oxidase (EC 1.4.3.4) was purified approx. 115-fold from the soluble fraction of bovine dental pulp (which is a pure connective tissue), by (NH 4) 2SO 4 fractionation (40–80% saturation), and DEAE-cellulose and Sephadex G-200 chromatographies. Bovine serum amine oxidase was also purified to the same extent, and the properties of both amine oxidases were compared. The dental pulp amine oxidase had an optimum pH between 8 and 9 and an approximate mol. wt. of 170 000. The dental pulp enzyme was inhibited by cuprizone, p- chloromercuribenzoate , iproniazid, β-aminopropionitrile, and lysine-vasopressin. The inhibition by iproniazid was reversed by the addition of pyridoxal phosphate. The dental pulp enzyme oxidized preferentially polyamines (spermine and spermidine), benzylamine, and peptidyllysine such as lysine-vasopressin and prolyllysylglycinamide, but did not oxidize collagen and elastin substrates. The properties of bovine serum amine oxidase were similar to those of dental pulp amine oxidase, but the serum enzyme was almost inactive towards lysine-vasopressin.
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