NO-Stimulated NAD-Dependent Modification of GAPDH

The 39-kDa protein identified as a common substrate for NO-stimulated NAD -dependent modification, was purified from human platelets (Dim- 

Additional experiments to characterize NO-catalyzed modification of GAPDH established the following  

Free [ P]ADP-ribose, derived from NAD, does not serve as a GAPDH-modifying agent (Dimmeler and Brune, 1992). 

NAD+-dependent NO-stimulated reactions apparently are not restricted to GAPDH modification. In human neutrophils actin becomes ADP-ribosylated when [ P]NAD is used in the presence of NO (Clancy et al., 

The NAD -dependent modification of GAPDH originally was thought to be identical to mono-ADP-ribosylation. Although NO-induced GAPDH modification resembles some features of ADP-ribosylation reactions, conditions for optimal protein modification are different from those in the toxin- 

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