Connective tissue amine oxidase. I. Purification of bovine aorta amine oxidase and its comparison with plasma amine oxidase

Abstract

1. 1. Bovine plasma and aorta amine oxidase (amine: O 2 oxidoreductase (deaminating), EC 1.4.3.4) were purified approx. 60- and 170-fold, respectively. The aorta enzyme appeared to be non-mitochondrial, did not catalyze the oxidation of common short chain diamines and, in general, possessed properties previously described for plasma amine oxidase. 2. 2. In the n-alkylamine series, CH 3(CH 2) nCH 2NH 2, the longer chain homologues were bound more tenaciously by both enzymes than the short chain homologues. 3. 3. The aorta enzyme was inhibited by chelating agents and activity could be partially restored by addition of Cu 2+. Activity was lost when the aorta enzyme was incubated in the presence of cyanide, hydroxylamine, semicarbazide, isoniazid and iproniazid. 4. 4. Preparations of amine oxidase from aorta catalyzed the oxidation of peptidyl lysine when lysine-vasopressin was used as substrate, but the plasma enzyme was inactive. The polyamines, spermine and spermidine, also served as substrates for the aorta enzyme and, relative to benzylamine, they were oxidized at the same rates as when the oxidation was catalyzed by the plasma amine oxidase.