Purification and characterization of cysteic acid and cysteine sulfinic acid decarboxylase and L-glutamate decarboxylase from bovine brain.
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چکیده
منابع مشابه
Purification of aromatic L-amino acid decarboxylase from bovine brain with a monoclonal antibody.
Aromatic L-amino acid decarboxylase was purified from bovine brain for the first time by affinity chromatography using a monoclonal antibody to the enzyme, and it was compared with the decarboxylase purified from bovine adrenal medulla by the same procedure. The monoclonal antibody was produced from a hybridoma established for the enzyme highly purified from bovine adrenal medulla. The Mr value...
متن کاملBrain 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...
متن کاملPartial 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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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1982
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.79.14.4270