Ontology highlight
ABSTRACT:
SUBMITTER: Bu DF
PROVIDER: S-EPMC48607 | biostudies-other | 1992 Mar
REPOSITORIES: biostudies-other
Bu D F DF Erlander M G MG Hitz B C BC Tillakaratne N J NJ Kaufman D L DL Wagner-McPherson C B CB Evans G A GA Tobin A J AJ
Proceedings of the National Academy of Sciences of the United States of America 19920301 6
We report the isolation and sequencing of cDNAs encoding two human glutamate decarboxylases (GADs; L-glutamate 1-carboxy-lyase, EC 4.1.1.15), GAD65 and GAD67. Human GAD65 cDNA encodes a Mr 65,000 polypeptide, with 585 amino acid residues, whereas human GAD67 encodes a Mr 67,000 polypeptide, with 594 amino acid residues. Both cDNAs direct the synthesis of enzymatically active GADs in bacterial expression systems. Each cDNA hybridizes to a single species of brain mRNA and to a specific set of rest ...[more]