Some characteristics of glutamic acid decarboxylase of chick ampullary cristae.

In a previous study, it was demonstrated that enzyme-mediated gamma-aminobutyric acid (GABA) synthesis occurs in the vestibule of the chick inner ear. As deeper knowledge of the properties of its synthesizing enzyme might contribute to the understanding of the role of GABA in inner ear function, some characteristics of glutamate decarboxylase (GAD) were studied in chick isolated ampullary cristae under conditions in which 14CO2 release from [1-14C]glutamate and [14C]GABA formation from [U-14C]glutamate for estimating GAD activity were equal. It was found that Km for glutamate is 5 mM and that the enzyme pH optimum is 7.3. These values fall within the range described for the corresponding enzyme in nervous tissue of other species. Pyridoxal phosphate (PLP) activates the enzyme and aminooxyacetic acid inhibits it, the same as these agents activate or inhibit GAD from several nervous tissue sources. 2-Mercaptoethanol shows some protection from inactivation of the PLP-dependent enzyme and Triton X-100 exerts some inhibition of vestibular GAD activity, as previously shown in other nervous tissue preparations. Although its cellular localization is at present uncertain, these results indicate that GAD of chick vestibular tissue possesses properties resembling those of the brain enzyme and might be controlled in a manner similar to that of GAD in brain, thus possibly participating in the regulation of inner ear function.