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- W1437701234 abstract "The enzymatic phosphorylation of RNA or DNA occurs at available 5 ' -hydroxyl ends of the polynucleotide chain. This reaction is conveniently measured by the incorporation of 32 P from γ- 32 P-labeled ATP into an acid-insoluble form. The enzyme, polynucleotide 5 ' -hydroxyl kinase, has been detected in the extracts of phage-infected Escherichia coli and rat liver nuclei. The chapter discusses the purification of kinase from Escherichia coli B infected with T2 and 3, properties of enzyme, and properties of the kinase preparation. The kinase preparation is relatively stable at low temperatures. The final enzyme fraction retained all its activity after 5 months at 0° at a protein concentration of 1.4 μg/ml. Because of the variable effects of freezing and thawing, all enzyme fractions were stored in ice at 0°. In the absence of substrates, the enzyme shows a marked temperature lability even at 25°. The following enzyme activities have been checked as contaminants of the final enzyme preparation (Bio-Rex eluate fraction)—ATPase, DNase, diesterase, RNase, and a specific 3 ' -deoxynucleotidase. The kinase activity shows a broad pH optimum in the range of pH 6–9; at pH 5 and 9.5, the rate was reduced by 50%. The kinase is completely dependent on the presence of a divalent metal for activity. The metal requirement is satisfied by a number of metals, such as Mg ++ , Mn ++ , Zn ++ , and Co ++ , all of which are equally active at saturating concentrations. At all stages in purification, both RNA and DNA containing 5 ' -hydroxyl ends are phosphate group acceptors. The ratio of kinase activity with these two different polynucleotides is constant during purification; partial inactivation of kinase activity measured with DNA is identical with RNA as aceeptor." @default.
- W1437701234 created "2016-06-24" @default.
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- W1437701234 date "1968-01-01" @default.
- W1437701234 modified "2023-09-27" @default.
- W1437701234 title "[110] Polynucleotide 5′-hydroxyl kinase" @default.
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- W1437701234 doi "https://doi.org/10.1016/0076-6879(67)12134-4" @default.
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