期刊
PROTEIN EXPRESSION AND PURIFICATION
卷 67, 期 2, 页码 113-119出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2009.05.002
关键词
Capping protein; CARMIL; Affinity matrix; CAH3 domain
类别
资金
- Intramural NIH HHS [Z99 HL999999] Funding Source: Medline
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. Published by Elsevier Inc.
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