title: Nucleic acid enzymology of extremely halophilic bacteria. Halobacterium cutirubrum polynucleotide phosphorylase.
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: D002247:Carbon Isotopes; D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D006217:Halobacterium / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008345:Manganese; D008970:Molecular Weight; D010710:Phosphates; D010759:Phosphorus Isotopes; D011506:Proteins / Q000032:analysis; D012316:RNA Nucleotidyltransferases / Q000302:isolation & purification*; D012965:Sodium Chloride; D013053:Spectrophotometry; D014732:Vibration
chemical_list: D002247:Carbon Isotopes; D010710:Phosphates; D010759:Phosphorus Isotopes; D011506:Proteins; D008345:Manganese; D012965:Sodium Chloride; D012316:RNA Nucleotidyltransferases