Brain L-Glutamate Decarboxylase

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Brain Glutamate Decarboxylase

Glutamate decarboxylase (glutamate 1-carboxylyase, EC 4.1.1.15, GAD)* IS the major, rate-limiting enzyme in brain for synthesizing gamma-aminobutyric acid (GABA). Total GAD activity in brain is 10-20 times greater than the observed rate of GABA synthesis (Collins, 1972; Matsui and Deguchi, 1977; Casu and Gale, 1981), indicating that GAD operates at only a fraction of its capacity. Although othe...

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Brain L-glutamate decarboxylase: purification and subunit structure.

Glutamate decarboxylase (GDCase; L-glutamate-1-carboxy-lyase, EC 4.1.1.15) was purified from whole rat brain approximately equal to 1300-fold to apparent homogeneity with a specific activity of 2.4 units per mg of protein by a combination of column chromatographies on DEAE-cellulose, hydroxylapatite, and gel filtration, and preparative nondenaturing polyacrylamide gel electrophoresis. The purif...

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Partial Cloning and Nucleotide Sequencing of Glutamate Decarboxylase Gene Isoform 65 from Human Brain

Background: Gamma -aminobutyric acid (GABA), a non-protein amino acid acts as an inhibitory neurotransmitter in the central nervous system of mammalians. The glutamate decarboxylase (GAD) is responsible for the conversion of L-glutamate to GABA. The human brain has two isoforms of this enzyme, GAD65 and GAD67 that differ in molecular weight, amino acid sequence, antigenicity, cellular location ...

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partial cloning and nucleotide sequencing of glutamate decarboxylase gene isoform 65 from human brain

background: gamma -aminobutyric acid (gaba), a non-protein amino acid acts as an inhibitory neurotransmitter in the central nervous system of mammalians. the glutamate decarboxylase (gad) is responsible for the conversion of l-glutamate to gaba. the human brain has two isoforms of this enzyme, gad65 and gad67 that differ in molecular weight, amino acid sequence, antigenicity, cellular location ...

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A membrane form of brain L-glutamate decarboxylase: Identification, isolation, and its relation to insulin-dependent diabetes mellitus

A membrane form of L-glutamate decarboxylase (GAD) was identified and purified to apparent homogeneity from hog brain. The purified GAD was established as an integral membrane protein by phase-partitioning assay, charge-shift electrophoresis, and chromatography on a hydrophobic interaction column. This membrane GAD has a native molecular mass of 96 ± 5 kDa and is a homodimer of 48 ± 3-kDa subun...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1995

ISSN: 0021-9258

DOI: 10.1074/jbc.270.12.6464