| 胆碱脱氢酶的N端氨基酸序列测定 |
| |
| 引用本文： | 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 |
| |
| 作者姓名： | 傅晓红 林其谁 |
| |
| 作者单位： | 中国科学院上海生物化学研究所，分子生物学国家重点实验室，上海 200031;中国科学院上海生物化学研究所，分子生物学国家重点实验室，上海 200031 |
| |
| 基金项目： | 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.
|
| 关 键 词： | 胆碱脱氢酶，电转移，一级结构，同源性 |
| 收稿时间： | 1996-03-21 |
| 修稿时间： | 1996-06-26 |
Amino Terminal Sequence of Choline Dehydrogenase |
| |
| FU Xiaohong and LIN Qishui. Amino Terminal Sequence of Choline Dehydrogenase[J]. Progress In Biochemistry and Biophysics, 1997, 24(2): 186-189 |
| |
| Authors: | FU Xiaohong and LIN Qishui |
| |
| Affiliation: | State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry, Academia Sinica, Shanghai 200031, China;State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry, Academia Sinica, Shanghai 200031, China |
| |
| Abstract: | 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. |
| |
| Keywords: | choline dehydrogenase electroblotting primary sequence homology |
| 本文献已被 CNKI 维普 等数据库收录！ |
| 点击此处可从《生物化学与生物物理进展》浏览原始摘要信息 |
|
点击此处可从《生物化学与生物物理进展》下载全文 |
