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通过赖氨酸残基的可逆修饰实现蛋白质与核蛋白复合物的快速分离。

Ready separation of proteins from nucleoprotein complexes by reversible modification of lysine residues.

作者信息

Shetty J K, Kinsella J E

出版信息

Biochem J. 1980 Oct 1;191(1):269-72. doi: 10.1042/bj1910269.

Abstract

Modification of proteins with citraconic anhydride altered the electrostatic relationship between cationic epsilon-NH3+ groups of lysine residues of proteins and anionic phosphate groups of nucleic acids, thereby destabilizing the nucleoprotein complex. This procedure facilitated the separation of proteins from nucleic acids at pH4-4.2. The modifying groups were then deacylated from the proteins under acidic conditions (pH3-6) at 30 degrees C.

摘要

用柠康酸酐修饰蛋白质,改变了蛋白质赖氨酸残基的阳离子ε-NH3+基团与核酸阴离子磷酸基团之间的静电关系,从而破坏了核蛋白复合物的稳定性。此方法有助于在pH4 - 4.2条件下从核酸中分离蛋白质。然后在30℃的酸性条件(pH3 - 6)下,将修饰基团从蛋白质上去酰化。

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本文引用的文献

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Reversible blocking of amino groups with citraconic anhydride.
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