Purification and Properties of Pyrimidine Nucleoside Monophosphate Kinase from Bakers Yeast
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概要
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Pyrimidine nucleoside monophosphate kinase was purified from bakers yeast to 280-fold. The molecular weight of the enzyme was calculated to be 26, 000 by gel filtration. With ATP as a phosphate donor, UMP was the most active phosphate acceptor. Besides UMP, the kinase also phosphorylated CMP, dCMP and dUMP. Km values for UMP, CMP, dCMP and dUMP were 0.052, 0.071, 0.54 and 8.5mM, respectively. The kinase was activated by preincubation with dithiothreitol. The extent of the activation depended on the concentration of dithiothreitol and incubation time. HgCl2, p-CMB and N-ethylmaleimide inhibited this enzyme.
- 社団法人 日本農芸化学会の論文
著者
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Tochikura Tatsurokuro
Department Of Agricultural Chemistry Kyoto University
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Kohno Hirao
Department Of Hygiene Kansai Medical University
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TOCHIKURA Tatsurokuro
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
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KUMAGAI Hidehiko
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University
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