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Purification and characterization of the deoxynucleoside monophosphate kinase of bacteriophage T5

机译:T5噬菌体脱氧核苷单磷酸激酶的纯化与鉴定

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摘要

Deoxynucleoside monophosphate kinase (dNMP kinase) of bacteriophage T5 (EC 2.7.4.13) was purified to apparent homogeneity from phage-infected Escherichia coli cells. Electrophoresis in sodium dodecyl sulfate-polyacrylamide gel showed that the enzyme has a molecular mass of about 29 kDa. The molecular mass of dNMP kinase estimated by analytical equilibrium ultracentrifugation turned out to be 29.14 +/- 3.03 kDa. These data suggest that the enzyme exists in solution as a monomer. The isoelectric point of dNMP kinase was found to be 4.2. The N-terminal amino acid sequence, comprising 21 amino acids, was determined to be VLVGLHGEAGSGKDGVAKLII. A comparison of this amino acid sequence and those of known enzymes with a similar function suggests. the presence of a nucleotide-binding site in the sequenced region. (C) 2002 Elsevier Science (OSA). All rights reserved. [References: 30]
机译:从噬菌体感染的大肠杆菌细胞中纯化出噬菌体T5(EC 2.7.4.13)的脱氧核苷单磷酸激酶(dNMP激酶),使其具有明显的同质性。十二烷基硫酸钠-聚丙烯酰胺凝胶中的电泳表明该酶的分子量约为29 kDa。通过分析平衡超速离心法估计的dNMP激酶的分子量为29.14 +/- 3.03kDa。这些数据表明该酶以单体形式存在于溶液中。发现dNMP激酶的等电点为4.2。包含21个氨基酸的N端氨基酸序列被确定为VLVGLHGEAGSGKDGVAKLII。建议将该氨基酸序列与已知功能相似的酶进行比较。在测序区域中存在核苷酸结合位点。 (C)2002 Elsevier Science(OSA)。版权所有。 [参考:30]

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