THE OXIDATION OF GLYCINE BY d-AMINO ACID OXIDASE IN EXTRACTS OF MAMMALIAN CENTRAL NERVOUS TISSUE |
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Authors: | Wilhelmina J de Marchi G A R Johnston |
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Institution: | Department of Physiology, Australian National University, Canberra, Australia |
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Abstract: | Abstract— 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. |
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