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Nitric Oxide Stimulates Auto-ADP-Ribosylation of Glyceraldehyde-3-Phosphate Dehydrogenase

Nitric oxide generation in brain cytosolic fractions markedly enhances ADP-ribosylation of a single 37-kDa protein. By utilizing a biotinylated NAD and avidin affinity chromatography, we purified this protein. Partial amino acid sequencing establishes its identity as glyceraldehyde-3-phosphate... Full description

1st Person: Zhang, Jie
Additional Persons: Snyder, Solomon H. verfasserin
Source: in Proceedings of the National Academy of Sciences of the United States of America Vol. 89, No. 20 (1992), p. 9382-9385
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Type of Publication: Article
Language: English
Published: 1992
Keywords: research-article
Biochemistry
Nitroarginine
Glutamate Neurotoxicity
cGMP
Biotinylated NAD
Online: Volltext
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520 |a Nitric oxide generation in brain cytosolic fractions markedly enhances ADP-ribosylation of a single 37-kDa protein. By utilizing a biotinylated NAD and avidin affinity chromatography, we purified this protein. Partial amino acid sequencing establishes its identity as glyceraldehyde-3-phosphate dehydrogenase (GAPDH). This is further confirmed by detection of GAPDH enzymatic activity in the purified 37-kDa protein. GAPDH is ADP-ribosylated in the absence of brain extract. This auto-ADP-ribosylation is enhanced by nitric oxide generation. ADP-ribosylation appears to involve the cysteine where NAD interacts with GAPDH so that ADP-ribosylation likely inhibits enzymatic activity. Such inhibition may play a role in nitric oxide-mediated neurotoxicity. 
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653 |a Glutamate Neurotoxicity 
653 |a cGMP 
653 |a Biotinylated NAD 
700 1 |a Snyder, Solomon H.  |e verfasserin  |4 aut 
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