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Structure and function ofl-glutamate decarboxylase

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Abstract

Membrane boundl-glutamate decarboxylase (GAD) has been solubilized and partially purified from hog brain. The solubilized GAD appears to exist in two forms, α and β, differing in their size and electrophoretic mobility. The α form has similar mobility as that of the soluble GAD in 7.5% and 5–25% gradient polyacrylamide gel electrophoresis suggesting that they are similar in size and charge. In addition, gene encoding for mouse brain GAD has been cloned and characterized. Mouse brain GAD cDNA consists of two DNA fragments with 1.6 and 1.0 Kb. The 1.6 and 1.0 Kb fragments contain 1657 and 974 bP, respectively. The significance of multiple forms of GAD is also discussed.

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Authors and Affiliations

  1. Department of Physiology and Cell Biology, University of Kansas, Lawrence, KS

    Jang-Yen Wu, Jun Bao, Britto nathan & Elliott Wu

  2. Department of Cell Biology, Baylor College of Medicine, Houston, TX

    Whei-Mei Huang & Lori Reed-Fourquet

  3. Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan, ROC

    Jang-Yen Wu & Wuhong Tsai

Authors
  1. Jang-Yen Wu
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  2. Whei-Mei Huang
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  3. Lori Reed-Fourquet
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  4. Jun Bao
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  5. Britto nathan
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  6. Elliott Wu
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  7. Wuhong Tsai
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Special issue dedicated to Dr. Eugene Roberts.

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Wu, JY., Huang, WM., Reed-Fourquet, L. et al. Structure and function ofl-glutamate decarboxylase. Neurochem Res 16, 227–233 (1991). https://doi.org/10.1007/BF00966085

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