胆碱脱氢酶的N端氨基酸序列测定  

Amino Terminal Sequence of Choline Dehydrogenase.

作　　者：傅晓红[1] 林其谁[1] 

机构地区：[1]中国科学院上海生物化学研究所

出　　处：《生物化学与生物物理进展》1997年第2期186-189,共4页Progress In Biochemistry and Biophysics

基　　金：国家自然科学基金资助项目

摘　　要：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.

关 键 词：胆碱脱氢酶 N端 氨基酸 序列测定 

分 类 号：Q554.03[生物学—生物化学]