Abstract
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.
Keywords
Glyceraldehyde 3-phosphate dehydrogenaseNAD+ kinaseBiochemistryNitric oxideDehydrogenaseBiotinylationADP-ribosylationChemistryEnzymeCysteine
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Publication Info
- Year
- 1992
- Type
- article
- Volume
- 89
- Issue
- 20
- Pages
- 9382-9385
- Citations
- 285
- Access
- Closed
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Cite This
J Zhang,
Solomon H. Snyder
(1992).
Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase..
Proceedings of the National Academy of Sciences
, 89
(20)
, 9382-9385.
https://doi.org/10.1073/pnas.89.20.9382
Identifiers
- DOI
- 10.1073/pnas.89.20.9382