Properties of poly(ADP-ribose) glycohydrolase purified from pig testis nuclei

Archives of Biochemistry and Biophysics
H Abe, S Tanuma

Abstract

A poly(ADP-ribose) glycohydrolase was purified more than 5,000-fold to apparent homogeneity from pig testis nuclei with a yield of 16%. A protein band, whose molecular mass (Mr) was estimated to be 58,000, detected by SDS-polyacrylamide gel electrophoresis of the purified preparation, was shown to have glycohydrolase activity upon assay by the renaturation method. A native Mr of 51,000 was determined by gel permeation. This polypeptide is a basic protein with a pI value of 8.8. The mode of hydrolysis of poly(ADP-ribose) [(ADP-ribose)n] by this enzyme is exoglycosidic, yielding ADP-ribose as the final product. The Km value for (ADP-ribose)n (average chain length, n = 15) is 5.4 microM and the Vmax of its hydrolysis is 34.5 micromol x min(-1) x mg protein(-1). The optimum pH for enzyme activity is 7.2. Low concentrations (50 approximately 150 mM) of monovalent salts stimulate the enzyme activity. The poly(ADP-ribose) glycohydrolase present in pig testis nuclei has some properties different from either nuclear poly(ADP-ribose) glycohydrolase (type I) or cytoplasmic poly(ADP-ribose) glycohydrolase (type II), purified previously from several tissues including pig thymus, guinea pig liver, calf thymus, human erythrocytes, and placent...Continue Reading

Citations

May 10, 2000·Bioscience, Biotechnology, and Biochemistry·S OgataH Taguchi
Jul 20, 2001·Experimental Cell Research·L DavidovicG G Poirier
Jun 10, 2019·Biochemical Pharmacology·Sei-Ichi TanumaHideaki Abe
Jul 18, 1997·Biochemical and Biophysical Research Communications·H MarutaS Tanuma

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