SUMMARY: Polynucleotide phosphorylase has been purified from the cyanobacterium sp. MAC. The enzyme requires a divalent cation such as Mg, has a pH optimum of 10·5 and catalyses the polymerization of ADP into polynucleotide in a primer-independent reaction at a rate of 2 μmol min (mg protein). It has an apparent native of 215000–240000. Non-denaturing polyacrylamide activity gels reveal a heterogeneous pattern of active bands similar to those previously observed with the corresponding enzyme from , while SDS-denaturing activity gels reveal a single band of activity of 91000 in both crude extracts and the most highly purified fraction. Activity has also been demonstrated in a cetyltrimethyl-ammonium bromide non-denaturing activity gel. By analogy with other known polynucleotide phosphorylases, the enzyme is probably a trimer of the 91000- subunit.


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