1887

Abstract

Polynucleotide phosphorylase activity was demonstrated in free-living and the symbiotic bacteroid forms of and in free-living . Crude extracts of -28 catalysed the polymerization of 3·0 mol ADP (mg protein) h. The polynucleotide phosphorylase activity of symbiotic was about 50 % of that of free-living and remained almost constant throughout the development of the nodules. Partially-purified fractions of free-living -28 catalysed the polymerization of ribonucleoside diphosphates, the phosphorolysis of synthetic homopolymers and natural heteropolymers, and the -phosphate exchange reaction. The enzyme had a pH optimum of 8·0 and had an obligatory requirement for Mg for maximum activity. The phosphorylase was not highly primer-dependent, had low specificity for guanosine-containing substrates, and exhibited cooperative-type kinetics.

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1977-10-01
2021-08-04
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