Purification and properties of vaccinia virus DNA-dependent RNA polymerase.
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Cations, Monovalent↗
Biomedical subjects
S Shuman
Publications and source records attributed to S Shuman.
5'-Hydroxyl polyribonucleotide kinase from HeLa cell nuclei. Purification and properties.
An enzyme, 5'-hydroxyl polyribonucleotide kinase, which catalyzes the phosphorylation of 5'-hydroxyl ends of RNA in the presence of ATP, has been isolated from extracts of HeLa cell nuclei. The kinase requires a divalent cation (Mg2+ or Mn2+) for activity, has an alkaline pH optimum, and is sensitive to the sulfhydryl antagonist N-ethylmaleimide. 5'-hydroxyl terminated polydeoxyribonucleotides are phosphorylated much less efficiently than the 5'-hydroxyl terminated polyribonucleotides, and the kinase preparation is inactive on ribonucleoside 3'-monophosphates. Enzyme activity is inhibited by ADP and by pyrophosphate. The sedimentation coefficient of the kinase is estimated to be 5.6 S from glycerol gradient centrifugation.
Cations, Divalent↗
Copper ion binding and enzyme inhibitory properties of the antithyroid drug methimazole.
The antithyroid drug, methimazole (1-methyl-2-thiolimidazole), is a powerful chelator of cupric ion. This is reflected in its ability to selectively inhibit certain copper oxidases. Uricase, ascorbic oxidase and monoamine oxidase are not affected. Ceruloplasmin oxidase is slightly inhibited and tyrosinase is markedly inhibited by methimazole.
Ascorbate Oxidase↗