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学科主题: 药学
题名:
Interactions of KChIP4a and its mutants with Ca2+ or Kv4.3 N-terminus by affinity capillary electrophoresis
作者: Li, Meina1,2; Lei, Lei1,3; Jia, Linghan1,3; Ling, Xiaomei1,2; Zhang, Jianmei1,2; Zhao, Yiran1,2; Wang, KeWei1,3
关键词: ACE ; Interaction ; Ca2+ ; KChIPs ; KvN
刊名: ANALYTICAL BIOCHEMISTRY
发表日期: 2014-03-15
DOI: 10.1016/j.ab.2013.12.015
卷: 449, 页:99-105
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemical Research Methods ; Biochemistry & Molecular Biology ; Chemistry, Analytical
研究领域[WOS]: Biochemistry & Molecular Biology ; Chemistry
关键词[WOS]: POTASSIUM CHANNELS ; BINDING CONSTANTS ; K+ CHANNELS ; MODULATION ; PROTEINS ; SUBUNITS ; DOMAINS
英文摘要:

The specific binding of auxiliary Kv channel-interacting proteins (KChIPs) to the N terminus of Kv4 poreforming alpha-subunits results in modulation of gating properties, surface expression, and subunit assembly of Kv4 channels. However, the interactions between KChIPs and Kv4 remain elusive. Thus, affinity capillary electrophoresis (ACE) was employed to quantitatively evaluate the interactions between KChIPs and Kv4.3 N terminus (KvN) and between KChIP4a/related mutants and Ca2+ for the first time. The mobility ratio, derivatives calculated from the mobility shift method, was used to deduce the binding constants (K-b). As a result, the binding constants for KChIP4a/KvN and KChIP1/KvN complexes were (8.32 +/- 1.66) x 10(6) L mol(-1) and (5.26 +/- 0.71) x 10(6) L mol(-1), respectively. In addition, in the presence of calcium (10 mu mol L-1), the binding constant of KChIP4a/KvN increased to (6.72 +/- 1.66) x 10(7) L mol(-1). In addition, the binding constant of KChIP4a with Ca2+ was (7.1 +/- 1.5) x 10(7) L mol(-1). Besides, studies on the effect of truncated mutants revealed that the third EF hand of KChIP4a was related to high-affinity binding with Ca2+, and the integrity of the molecular structure of KChIP4a was important for Ca2+ binding. This method profits from small samples, rapid analysis, and simple operation without being time-consuming. (C) 2013 Elsevier Inc. All rights reserved.

语种: 英语
所属项目编号: 30872292 ; 90813025 ; 81072612 ; 81373372 ; SKL2012004 ; 20110001110021 ; 2013CB531300 ; 81221002
项目资助者: National Natural Science Foundation of China ; Open Foundation of State Key Laboratory of Natural and Biomimetic Drugs ; Specialized Research Fund for the Doctoral Program of Higher Education of China ; Ministry of Science and Technology of China ; National Science Foundation of China
WOS记录号: WOS:000332816100014
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内容类型: 期刊论文
URI标识: http://ir.bjmu.edu.cn/handle/400002259/66321
Appears in Collections:北京大学药学院_期刊论文

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作者单位: 1.Peking Univ, Sch Pharmaceut Sci, State Key Lab Nat & Biomimet Drugs, Beijing 100191, Peoples R China
2.Peking Univ, Sch Pharmaceut Sci, Dept Pharmaceut Anal, Beijing 100191, Peoples R China
3.Peking Univ, Dept Mol & Cellular Pharmacol, Sch Pharmaceut Sci, Beijing 100191, Peoples R China

Recommended Citation:
Li, Meina,Lei, Lei,Jia, Linghan,et al. Interactions of KChIP4a and its mutants with Ca2+ or Kv4.3 N-terminus by affinity capillary electrophoresis[J]. ANALYTICAL BIOCHEMISTRY,2014,449:99-105.
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