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THE OXIDATION OF GLYCINE BY d ‐AMINO ACID OXIDASE IN EXTRACTS OF MAMMALIAN CENTRAL NERVOUS TISSUE
Author(s) -
Marchi Wilhelmina J.,
Johnston G. A. R.
Publication year - 1969
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.1471-4159.1969.tb10374.x
Subject(s) - glycine , cerebellum , biochemistry , amino acid , d amino acid oxidase , cerebral cortex , alanine , spinal cord , serine , central nervous system , oxidase test , glutamate receptor , chemistry , biology , enzyme , endocrinology , receptor , neuroscience
— Glycine was a substrate for d ‐amino acid oxidase purified from extracts of cat spinal cord and sheep cerebellum. d ‐Aspartate and N ‐methyl‐ d ‐aspartate were oxidized at a rate similar to that of glycine by the purified sheep cerebellum extract; d ‐α‐alanine and d ‐serine were oxidized appreciably faster than glycine, while GABA and d ‐glutamate were not oxidized at a measurable rate. p ‐Mercuribenzoate and kojate inhibited the oxidation of glycine by the purified sheep cerebellum extract. d ‐Amino acid oxidase activity was higher in the grey than in the white matter of cat spinal cord, while the reverse was true for the cerebral cortex; the activity in the cord and cerebral cortex was much lower than that in the cerebellum.