Substrate specificity of amine oxidase

The tyramine oxidase activity of liver extracts found by Hare (1), the aliphatic amine oxidase activity of brain, kidney, and liver extracts observed by Pugh and Quastel (2), and the adrenalin oxidase activity of similar extracts noted by Blaschko, Richter, and Schlossman (3) were brought under a common enzyme view-point by the latter authors. They were able to show (4) that extracts of brain, instestine, kindey, and liver from a number of mammals or representatives of the birds, reptiles, amphibians, and fishes all acted to absorb oxygen in the presence of several amine substrates. Hare (1) had shown that tyramine and phenethylamine form ammonia in the course of such oxidations, and Richter (5) showed that an ethylamino and a dimethylamino compound, as well as a number of methylamino and amino compounds, all yield the corresponding alkyl-amines or ammonia in the enzymic oxidation. The conslusion that the demonstrated variey of such enzymic activity can be acribed to the presence of a single type pf amine oxidase was dependent in large part on observations that the relative activities of a preparation from one source on a series of substrates bear some relation to the relative activities exhibited by a preparation from another source. Further evidence depended on the action of certain amines as inihibitors and apparent competition between substrates when two oxidizable substrates are present in the system. The degree to which relative activities of different enzyme preparations were constant in a series of substrates was not good in the data reported, and the fact that Hare (1) had not been able to note activity of the liver preparations she used upon adrenalin as the substrate appeared to require special explanations