Identification in human erythrocytes of mono(ADP‐ribosyl) protein hydrolase that cleaves a mono(ADP‐ribosyl) Gi linkage
Authors:
- Sei-Ichi TanumaSTSei-Ichi Tanuma
- Hiroyoshi EndoHEHiroyoshi Endo
- 26 February 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 261 (2) , 381-384
Abstract
A novel enzymatic activity, the hydrolysis of linkages between mono(ADP‐ribose) and cysteine residues in Gi prepared by eukaryotic ADP‐ribosyl‐transferase C [(1988) J. Biol. Chem. 263, 5485‐5489] was found in the cytosol of human erythrocytes. The mono(ADP‐ribosyl) Gi hydrolase, tentatively named ADP‐ribosyI protein hydrolase C was partially purified by sequential chromatographies on DEAE‐cellulose and Blue Sepharose. This enzyme catalyzes the release of ADP‐ribose from mono(ADP‐ribosyl) Gi Its activity was enhanced by Ca2+ and inhibited by ADP‐ribose. The presence of this enzyme in eukaryotic cells suggests that endogenous mono(ADP‐ribosyl)ation of Gi is a reversible post‐translational modification.Keywords
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