THE OXIDATION OF GLYCINE BY d ‐AMINO ACID OXIDASE IN EXTRACTS OF MAMMALIAN CENTRAL NERVOUS TISSUE

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.