Abstract
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 optimun 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.
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