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Identification in human erythrocytes of mono(ADP‐ribosyl) protein hydrolase that cleaves a mono(ADP‐ribosyl) G i linkage
Author(s) -
Tanuma Sei-ichi,
Endo Hiroyoshi
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80597-c
Subject(s) - hydrolase , enzyme , chemistry , cytosol , biochemistry , transferase , adp ribosylation , cysteine , poly adp ribose polymerase , stereochemistry , nad+ kinase , polymerase
A novel enzymatic activity, the hydrolysis of linkages between mono(ADP‐ribose) and cysteine residues in G i 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) G i 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) G i Its activity was enhanced by Ca 2+ and inhibited by ADP‐ribose. The presence of this enzyme in eukaryotic cells suggests that endogenous mono(ADP‐ribosyl)ation of G i is a reversible post‐translational modification.