
doi: 10.1007/bf00966085
pmid: 1780025
Membrane bound L-glutamate decarboxylase (GAD) has been solubilized and partially purified from hog brain. The solubilized GAD appears to exist in two forms, alpha and beta, differing in their size and electrophoretic mobility. The alpha 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.
Base Sequence, Glutamate Decarboxylase, Octoxynol, Swine, Recombinant Fusion Proteins, Cell Membrane, Molecular Sequence Data, Brain, DNA, Polyethylene Glycols, Kinetics, Mice, Solubility, Animals, Electrophoresis, Polyacrylamide Gel
Base Sequence, Glutamate Decarboxylase, Octoxynol, Swine, Recombinant Fusion Proteins, Cell Membrane, Molecular Sequence Data, Brain, DNA, Polyethylene Glycols, Kinetics, Mice, Solubility, Animals, Electrophoresis, Polyacrylamide Gel
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