Assay and properties of glutamic acid decarboxylase in homogenates of crayfish nervous tissue
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,General Medicine,Physiology,Biochemistry
Reference80 articles.
1. Borohydride reduction of l-glutamate decarboxylase;Anderson;Archs Biochem. Biophys.,1965
2. Ultrastructure of nerve terminals and muscle fibers in denervated crayfish muscle;Atwood;Z. Zellforsch,1973
3. Paradoxical inhibition of phosphorylase by pyridoxal phosphate. I. Studies on the reaction of pyridoxal phosphate with a specific lysine residue of phosphorylase b;Avramovic-Zikic;J. biol. Chem.,1972
4. Paradoxical inhibition of phosphorylase by pyridoxal phosphate. II. Characterization of the pyridoxal phosphate-phorphorylase derivative;Avramovic-Zikic;J. biol. Chem.,1972
5. Assay of γ-aminobutyric acid and enzymes involved in its metabolism;Baxter,1972
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3. Block of glutamate decarboxylase decreases GABAergic inhibition at the crayfish synapses: possible role of presynaptic metabotropic mechanisms;Journal of Neurophysiology;1996-05-01
4. Long-term persistence of GAD activity in injured crayfish CNS tissue;Neurochemical Research;1987-11
5. Inhibition of crayfish glutamic acid decarboxylase by structural analogs of the substrate and product;Comparative Biochemistry and Physiology Part C: Comparative Pharmacology;1985-01
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