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Inverse relationship of the dehydrogenase and ADP-ribosylation activities in sodium-nitroprusside-treated glyceraldehyde-3-phosphate dehydrogenase is coincidental

Vaidyanathan, VV and Sastry, PS and Ramasarma, T (1993) Inverse relationship of the dehydrogenase and ADP-ribosylation activities in sodium-nitroprusside-treated glyceraldehyde-3-phosphate dehydrogenase is coincidental. In: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1203 (1). pp. 36-44.

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Official URL: http://dx.doi.org/10.1016/0167-4838(93)90033-N

Abstract

Incubation of glyceraldehyde-3-phosphate dehydrogenase (GAPD) with sodium nitroprusside (SNP) decreased its activity in concentration- and time-dependent fashion in the presence of a thiol compounds, with DTT being more effective than GSH. Both forward and backward reactions were effected. Coinciding with this, HgCl2-sensitive labelling of the protein by [32P]NAD+ also increased, indicating the stimulation of ADP-ribosylation. Treatment with SNP of GAPD samples from rabbit muscle, sheep brain and yeast inactivated the dehydrogenase activity of the three, but only the mammalian proteins showed ADP-ribosylation activity. The SNP-modified protein of rabbit muscle GAPD, freed from the reagent by Sephadex filtration showed a concentration-dependent restoration of the dehydrogenase activity on preincubation with DTT and GSH. Such thiol-treated preparations also gave increased ADP-ribosylation activity with DTT, and to a lesser extent with GSH. The SNP-modified protein was unable to catalyze this activity with the native yeast enzyme and native and heat-inactivated muscle enzyme. It was possible to generate the ADP-ribosylation activity in muscle GAPD, by an NO-independent mechanism, on dialysis in Tris buffer under aerobic conditions , and on incubating with NADPH, but not NADH, in muscle and brain, but not yeast, enzymes. The results suggest that the inverse relationship of the dehydrogenase and ADP-ribosylation activities is coincidental but not correlated

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Science.
Keywords: Glyceraldehyde-3-phosphate dehydrogenase;Sodium nitroprusside;Nitric oxide;ADP ribosylation,
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 11 Feb 2011 05:17
Last Modified: 11 Feb 2011 05:17
URI: http://eprints.iisc.ernet.in/id/eprint/35514

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