Sarkosyl is a good regeneration reagent for studies on vacuolar-type ATPase subunit interactions in Biacore experiments

被引：7

作者：

Rahman, Suhaila ^{[2
]}

Arai, Satoshi ^{[1
,2
]}

Saijo, Shinya ^{[2
,3
]}

Yamato, Ichiro ^{[2
]}

Murata, Takeshi ^{[1
,4
]}

机构：

[1] Chiba Univ, Dept Chem, Grad Sch Sci, Inage Ku, Chiba 2638522, Japan

[2] Tokyo Univ Sci, Dept Biol Sci & Technol, Noda, Chiba 2788510, Japan

[3] RIKEN SPring 8 Ctr, Sayo, Hyogo 6795148, Japan

[4] RIKEN Syst & Struct Biol Ctr, Yokohama, Kanagawa 2300045, Japan

来源：

ANALYTICAL BIOCHEMISTRY | 2011年 / 418卷 / 02期

关键词：

Surface plasmon resonance; Regeneration; Sarkosyl; Biacore; V-ATPase; SOLUBILIZATION; PURIFICATION; PROTEINS;

D O I：

10.1016/j.ab.2011.07.009

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Biacore is widely used for studies on protein-protein interaction in which regeneration is one of the most important steps. Here we introduce the anionic detergent sodium lauroyl sarcosinate (sarkosyl), which works satisfactorily as a regeneration reagent. After regeneration by the mild detergent, the subsequent binding experiment was reproducible without any degradation of the ligand. This regeneration condition can be employed for diverse combinations of ligand-analyte binding interactions and optimized as required. (C) 2011 Elsevier Inc. All rights reserved.

引用

页码：301 / 303

页数：3

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