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CDH N端10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(adenylyl cyclase)、人甾体结合蛋白(oxysterol-binding protein)有很高同源性,但与大肠杆菌CDH并无明显的同源性.
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.
傅晓红,林其谁.胆碱脱氢酶的N端氨基酸序列测定[J].生物化学与生物物理进展,1997,24(2):186-189
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