Occurrence of (ADP-ribose)N glycohydrolase in human erythrocytes.
Chromatography of the cytosol of human erythrocytes on Blue Sepharose, S Sepharose, DEAE-cellulose and single-stranded DNA cellulose yielded a fraction which contained an (ADP-ribose)n glycohydrolase activity. The enzyme hydrolyzed (ADP-ribose)n in a fashion of exo-glycosidase. The native molecular weight of the enzyme was estimated to be 56,000 by gel filtration on Sepharose CL-6B. Its optimum pH was around 7.2. ADP-ribose, cAMP and monovalent salts inhibited the activity. Such characteristics established this glycohydrolase as being a cytosolic glycohydrolase II.
D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002855:Chromatography, Thin Layer; D004912:Erythrocytes / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000097:blood*; D006801:Humans; D006863:Hydrogen-Ion Concentration
D006026:Glycoside Hydrolases; C022407:poly ADP-ribose glycohydrolase