Abstract
Abstract— l‐Glutamic acid decarboxylase (GAD) was isolated from bovine cerebellum and purified approx 32‐fold by a combination of DEAE‐Sephadex chromatography and gel filtration. This preparation was purified electrophoretically. Rabbit antiserum against the electrophoretically purified bovine GAD was found to react with the decarboxylase of bovine cerebellum and mouse brain. Examination of GAD enzyme specific activity at various postnatal ages of developing mouse brain showed that an initial rise in GAD activity occurs at 6 days postnatally. followed by a rapid increase in enzymatic activity which reaches a maximum at 28 days postnatally. Quantitative immunoprecipitation of mouse GAD by rabbit anti‐GAD antisera indicated that the amount of GAD per brain increases 10‐fold over the period between 1 and 28 days postnatally. This increase coincides closely with the GAD enzyme activity profile. Therefore, the increase in GAD enzyme specific activity during the postnatal development of mouse brain represents an increase in the absolute amount of GAD enzyme protein.
Published Version
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