title: Immunoaffinity purification of l-glutamate decarboxylase.
abstract: A rapid and efficient immunoaffinity procedure for the purification of a new form of brain l-glutamate decarboxylase (GAD) is described. A well characterized monoclonal antibody against rat brain GAD is used as an affinity ligand. The GAD-anti-GAD complex is dissociated by a relatively gentle condition e.g. 0.2 M acetate buffer, pH 4 or 5. GAD preparations thus obtained are still enzymatically active and have a minimum molecular weight of 67,000 Da. The significance of this new form of GAD is also discussed.
authors.affiliation: Neuroscience Program and Department of Physiology and Anatomy, Milton S. Hershey Medical Center, Pennsylvania State University, Hershey, PA 17033 U.S.A.; Department of Physiology and Cell Biology, University of Kansas, Lawrence, KS 66045-2106, U.S.A.; Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan, Republic of China.
authors.forename: J Y
authors.initials: JY
authors.lastname: Wu
authors.forename: J Y
authors.initials: JY
authors.lastname: Liu
authors.forename: C T
authors.initials: CT
authors.lastname: Lin
authors.forename: D
authors.initials: D
authors.lastname: Evans
authors.forename: W H
authors.initials: WH
authors.lastname: Tsai