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.
MeSH terms
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Carbon Isotopes
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Centrifugation, Density Gradient
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Chromatography, Gel
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Halobacterium / enzymology*
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Hydrogen-Ion Concentration
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Manganese
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Molecular Weight
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Phosphates
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Phosphorus Isotopes
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Proteins / analysis
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RNA Nucleotidyltransferases / isolation & purification*
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Sodium Chloride
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Spectrophotometry
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Vibration
Substances
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Carbon Isotopes
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Phosphates
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Phosphorus Isotopes
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Proteins
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Manganese
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Sodium Chloride
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RNA Nucleotidyltransferases