胆碱脱氢酶的N端氨基酸序列测定

Amino Terminal Sequence of Choline Dehydrogenase.

采用SDS PAGE凝胶电泳及电转移方法 ,将增溶的鼠肝线粒体胆碱脱氢酶进一步纯化 ,且去掉增溶线粒体胆碱脱氢酶 (CDH)中所包含的大部分磷脂、去垢剂、辅基FAD等 .对进一步纯化的CDH进行了N端氨基酸序列测定 ,得到CDHN端 1 0个氨基酸残基序列为VAAAAGGGKD ,这一部分序列与小鼠CO5蛋白 (即补体C5的前体蛋白 )、大鼠腺苷酰 (基 )环化酶 (adenylylcyclase)、人甾体结合蛋白 (oxysterol bindingprotein)有很高同源性 。

Solubilized rat liver mitochondrial choline dehydrogenase was further purified by the SDS PAGE and electroblotting methods. Both the lipids and detergents etc. were removed during the process of purification. The amino terminal sequence of the purified CDH was determined , it was: VAAAAGGGKD. Although the sequence showed high homology with mouse CO5 protein, rat adenylyl cyclase and human oxysterol binding protein, there was no similarity with CDH of E.coli.