Expression of recombinant goldfish glutamic acid decarboxylase 65 and evidence for differential pH and PLP responsiveness compared to the human enzyme.

@article{Sardana2006ExpressionOR,
  title={Expression of recombinant goldfish glutamic acid decarboxylase 65 and evidence for differential pH and PLP responsiveness compared to the human enzyme.},
  author={Ravinder K Sardana and Rosalie Awad and John T Arnason and Vance L. Trudeau},
  journal={Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
  year={2006},
  volume={144 1},
  pages={94-100}
}
Glutamic acid decarboxylase (GAD) catalyzes the conversion of glutamate to gamma-aminobutyric acid (GABA) that acts as an important inhibitory neurotransmitter in the vertebrate brain, as well as in the regulation of neuroendocrine function. GAD65 and GAD67 are the two main isoforms that exist in vertebrates. The biochemical properties of recombinant forms of goldfish and human GAD65 were examined. The recombinant goldfish GAD65 (gfGAD65) was expressed at high levels using a maltose binding… CONTINUE READING