Abstract
An enzyme which catalyzed the hydrolytic removal of the 6-amino group of adenosine 5'-phosphosulfate (APS) into inosine 5'-phosphosulfate was purified from the marine red macroalga Gloioeltis furcata by means of salt fractionation, affinity, anion-exchange, and hydrophobic interaction chromatographies. The native enzyme had a M(r) of about 285000. Dissociation yielded a form with a M(r) of about 70000. The enzyme catalyzed the irreversible deamination of adenosine and its 5'-substituted compounds in addition to APS. Thus the enzyme seemed to be a nonspecific adenine nucleotide deaminase. Some properties were determined and compared with those of other nonspecific adenine nucleotide deaminases.
Original language | English |
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Pages (from-to) | 845-853 |
Number of pages | 9 |
Journal | Biochemistry International |
Volume | 23 |
Issue number | 5 |
Publication status | Published - 1991 Jun 20 |
ASJC Scopus subject areas
- Biochemistry