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Purification and properties of a mitochondrial NAD+ glycohydrolase.

Abstract：

:A 60- to 70-fold purification of an NAD+ glycohydrolase from the inner membrane of rat liver mitochondria to apparent homogeneity on sodium dodecyl sulfate (SDS)-polyacrylamide slab gel is described. The minimum molecular weight of the enzyme on polyacrylamide gels in the presence of SDS is around 62,000. The enzyme splits NAD+ to ADP-ribose and, presumably, nicotinamide. No phosphatase or phosphodiesterase activity is detected in the purified enzyme preparation. The enzyme shows high activity with NAD+ and moderate activity with NADP+ as substrates NAD(P)Hs are poor substrates. ATP and nicotinamide inhibit the enzyme. A possible participation of the enzyme in the mechanism of calcium release from rat liver mitochondria is discussed.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Moser B,Winterhalter KH,Richter C

doi

10.1016/0003-9861(83)90220-5

subject

Has Abstract

pub_date

1983-07-01 00:00:00

pages

358-64

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(83)90220-5

journal_volume

224

pub_type

杂志文章

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