In vitro phosphorylation of proteins tightly bound to DNA by protein kinase NII.

G Piccinini, M Bramucci, E Maccari, A Miano, D Amici, G L Gianfranceschi, E Cardellini
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引用次数: 3

Abstract

1. Highly purified DNA from calf thymus was phosphorylated with protein kinase NII. 2. Digestion with proteinase K of this DNA demonstrates proteins as phosphorylated component. 3. Gel filtration chromatography on Bio-Gel A-0.5m gel column shows a major protein peak between 50 and 70 kDa. 4. SDS gel electrophoresis, after hydrolysis, to digest completely DNA, shows three major phosphorylated bands corresponding to polypeptides of M(r) between 31 and 21 kDa. 5. After high voltage electrophoresis on TLC plates tryptic digested polypeptides show very similar phosphopeptides patterns.

蛋白激酶NII对DNA紧密结合蛋白的体外磷酸化作用。
1. 用蛋白激酶NII磷酸化小牛胸腺高度纯化的DNA。2. 用蛋白酶K消化这些DNA,证明蛋白质是磷酸化的成分。3.在Bio-Gel a -0.5m凝胶柱上进行凝胶过滤层析,发现主蛋白峰在50 ~ 70 kDa之间。4. 水解后的SDS凝胶电泳,完全消化DNA,显示出三个主要的磷酸化带,对应于31 - 21 kDa之间的M(r)多肽。5. 在TLC板上进行高压电泳后,胰蛋白酶消化多肽显示出非常相似的磷酸肽模式。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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