On peroxidase deanimation of amino acids

Abstract

The authors make a study of the possible catalyzing action of haemoglobinic peroxydase in the deamination of aminoacids through the action of hydrogen peroxide. For this purpose Solutions of different aminoacids in H2O2 a slightly acid medium, are mixed with others of haemoglobine and kept in contact for 24 hours at 35°. On proceeding to the determination of ammonium no positive results were obtained in the aminoacids under observation: glycocol, alanin, leucin, thyrosin, glutaminic and aspartic acids and asparagin. In the last named NH3 is separated, which must correspond to the amide group without any catalyzer assistence.

Previously it is ascertained that the H2O2 in a strong concentration and at 100° does not produce deamination in the aminoacids mentioned. As in the former instance, asparagin liberates ammonium, which must correspond to the amide group.