| Literature DB >> 5114973 |
Abstract
1. Polynucleotide phosphorylase was purified 200-fold from Halobacterium cutirubrum. 2. It is membrane-associated and can be solubilized by sonication. 3. The purified enzyme requires a high ionic strength for both stability and activity. 4. It is Mn(2+)-dependent, has all three typical polynucleotide phosphorylase activities and is specific for nucleoside diphosphates. 5. The enzyme is of low molecular weight.Entities:
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Year: 1971 PMID: 5114973 PMCID: PMC1176637 DOI: 10.1042/bj1210613
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857