Differences in some properties of newborn and adult brain glutamate decarboxylase

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Abstract
Some properties of glutamate decarboxylase (EC 4.1.1.15) activity in brain of newborn and adult mouse were studied comparatively. It was found that glutamate decarboxylase of the newborn brain was strongly inactivated by homogenization in hypotonic medium, centrifugation of isotonic sucrose homogenates, preincubation at 37°C or the addition of Triton‐X‐100, whereas the adult brain enzyme was practically unaffected by any of these conditions. It was also found that the newborn glutamate decarboxylase was less activated by pyridoxal 5′‐phosphate and less inhibited by pyridoxal 5′‐phosphate oxime‐O‐acetic acid, than the adult enzyme. These differences do not exist for brain dihydroxyphenylalanine decarboxylase (EC 4.1.1.26) and are not due to the release of inhibitors from the newborn brain. On the basis of the results obtained it is postulated that two forms of glutamate decarboxylase exist in brain: a newborn form, which is unstable and has high affinity for pyridoxal 5′‐phosphate, and an adult form, which is much more stable and has low affinity for pyridoxal 5′‐phosphate. The possible implications of these findings in the establishment of the σ‐aminobutyric acid dependent synaptic inhibitory mechanisms during development are discussed.