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Presence of Kynurenine Hydroxylase in Developing Rat Brain
Author(s) -
Battie Cynthia,
Verity M. Anthony
Publication year - 1981
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1981.tb01737.x
Subject(s) - monoamine oxidase , kynurenine , enzyme , cerebral cortex , biochemistry , tryptophan hydroxylase , endocrinology , chemistry , mitochondrion , medicine , cytochrome c oxidase , biology , tryptophan , serotonin , amino acid , serotonergic , receptor
Kynurenine‐3‐hydroxylase, an enzyme that is part of the degradative pathway for tryptophan, was present in the cerebral cortex of neonatal rats and exhibited a K m , for L‐kynurenine close to that of the liver enzyme. This enzyme was enriched in mitochondrial fractions isolated from cerebral cortices of neonatal rats by Ficoll‐sucrose gradient centrifugation, with some activity also present in synaptosomal fractions probably due to the mitochondrial content of synaptosomes since cytochrome c oxidase, another mitochondrial enzyme, had a similar distribution in the gradient. Kynurenine hydroxylase as well as monoamine oxidase, another mitochondrial enzyme, had increased specific activities in synaptosomal fractions isolated from 14‐day‐old rats compared to fractions from 8‐day‐old rats. Hypothyroidism, induced on the day of birth, resulted in increased activities of kynurenine hydroxylase and monoamine oxidase in synaptosomal fractions isolated from 14‐day‐old rats.