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FEBS Lett. 1995 Dec 27;377(3):530-4.

Identification and purification of a bovine liver mitochondrial NAD(+)-glycohydrolase.

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Institute of Biochemistry, University of Innsbruck, Austria.


Nonenzymatic ADP-ribosylation of mitochondrial proteins is thought to play a role in the regulation of Ca2+ efflux from mitochondria. It has been shown that intramitochondrial ADP-ribose is generated by a specific NAD(+)glycohydrolase, which catalizes hydrolysis of NAD+ to ADP-ribose and nicotinamide. We purified this enzyme from bovine liver mitochondrial membranes. The final preparation had a 1660-fold purified enzyme activity and contained a main protein band with an apparent molar mass of 32,000 in a SDS-polyacrylamide gel. The identity of this protein band with NAD(+)-glycohydrolase was verified by renaturation of its enzymatic activity. Partial amino acid sequence information was obtained from two enzyme fragments after proteolytic cleavage of the protein band in the SDS-polyacrylamide gel. Searches in protein databases revealed that an arginine ADP-ribosyl hydrolase harbours two stretches of amino acids that are highly similar to the partial NAD(+)-glycohydrolase sequences.

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