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通过电泳化学修饰蛋白质以提高其相对分子质量测定的准确性。

Chemical modification of proteins to improve the accuracy of their relative molecular mass determination by electrophoresis.

机构信息

Alcor BioSeparations LLC, Palo Alto, CA, USA.

出版信息

Electrophoresis. 2011 Oct;32(20):2893-7. doi: 10.1002/elps.201100141. Epub 2011 Sep 8.

DOI:10.1002/elps.201100141
PMID:21905048
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3516873/
Abstract

We studied the electrophoretic behavior of basic proteins (cytochrome c and histone III) and developed a carbamylation method that normalizes their electrophoretic size separation and improves the accuracy of their relative molecular mass determined electrophoretically. In capillary zone electrophoresis with cationic hitchhiking, native cytochrome c does not sufficiently bind cationic surfactants due to electrostatic repulsion between the basic protein and cationic surfactant. Carbamylation suppresses the strong positive charge of the basic proteins and results in more accurate relative molecular masses.

摘要

我们研究了碱性蛋白质（细胞色素 c 和组蛋白 III）的电泳行为，并开发了一种碳化方法，该方法可使它们的电泳大小分离正常化，并提高电泳测定的相对分子量的准确性。在阳离子随行的毛细管区带电泳中，由于碱性蛋白质与阳离子表面活性剂之间的静电排斥，天然细胞色素 c 不能充分结合阳离子表面活性剂。碳化抑制了碱性蛋白质的强正电荷，从而得到更准确的相对分子量。

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