Purification of capping protein using the capping protein binding site of CARMIL as an affinity matrix

Kirsten Remmert, Takehito Uruno, John A. Hammer

研究成果: ジャーナルへの寄稿学術誌査読

4 被引用数 (Scopus)

抄録

Capping protein (CP) is a ubiquitously expressed, heterodimeric actin binding protein that is essential for normal actin dynamics in cells. The existing methods for purifying native CP from tissues and recombinant CP from bacteria are time-consuming processes that involve numerous conventional chromatographic steps and functional assays to achieve a homogeneous preparation of the protein. Here, we report the rapid purification of Acanthamoeba CP from amoeba extracts and recombinant mouse CP from E. coli extracts using as an affinity matrix GST-fusion proteins containing the CP binding site from Acanthamoeba CARMIL and mouse CARMIL-1, respectively. This improved method for CP purification should facilitate the in vitro analysis of CP structure, function, and regulation.

本文言語英語
ページ(範囲)113-119
ページ数7
ジャーナルProtein Expression and Purification
67
2
DOI
出版ステータス出版済み - 10月 2009
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • バイオテクノロジー

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