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OBSERVATIONS ON THE SUBSTRATE SPECIFICITY OF AMINE OXIDASES
Author(s) -
BLASCHKO H.,
CHRUŚCIEL T. L.
Publication year - 1959
Publication title -
british journal of pharmacology and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0366-0826
DOI - 10.1111/j.1476-5381.1959.tb00258.x
Subject(s) - diamine oxidase , substrate (aquarium) , amine oxidase (copper containing) , substrate specificity , chemistry , amine oxidase , guinea pig , amine gas treating , biochemistry , enzyme , pig liver , horse , stereochemistry , organic chemistry , endocrinology , biology , ecology , paleontology
A number of compounds have been tested as substrates of, first, the amine oxidases of rabbit and guinea‐pig liver and of goat, pig, horse, and dog plasma and, second, the “diamine oxidase” of pig kidney. Of the three xylylenediamines [di(aminomethyl)benzenes] tested, m ‐xylylenediamine was found to be a substrate of the liver oxidase. All the plasma oxidases tested acted on both m ‐ and o ‐xylylenediamine. Both 3‐ and 4‐picolylamine (3‐ and 4‐aminomethylpyridine) were readily oxidized by the liver enzymes; all the plasma oxidases tested oxidized 2‐, 3‐, and 4‐picolylamine. 4‐Picolylamine was more rapidly oxidized by horse and dog plasma than any other substrate hitherto examined.