Poly ADP Ribose Glycohydrolase (PARG)

PARG had a calculated molecular mass of 111 kD, nearly twice the size of the 59-kD enzymatically active PARG isolated from bovine thymus. Using an activity gel assay of extracts from bacteria expressing PARG, the authors determined that cDNA encoded proteins of approximately 115 and 59 kD. The larger protein was sensitive to proteolysis, yielding a protein of approximately 59 kD.

The enzymatically active 59-kD PARG corresponded to the C-terminal portion of the protein. The authors suggested that proteolysis explains the presence of PARG activity with a molecular mass of approximately 74 and 59 kD in bovine thymus preparations, and previous reports of a 74-kD PARG in guinea pig liver and human placenta.