Sodium Dodecyl Sulfate Analogs as a Potential Molecular Biology Reagent

被引:9
作者
Arakawa, Tsutomu [1 ]
Niikura, Takako [2 ]
Kita, Yoshiko [1 ]
Akuta, Teruo [3 ]
机构
[1] Alliance Prot Labs, 13380 Pantera Rd, San Diego, CA 92130 USA
[2] Sophia Univ, Fac Sci & Technol, Dept Informat & Commun Sci, Tokyo 1028554, Japan
[3] Kyokuto Pharmaceut Ind Co Ltd, Res & Dev Div, 3333-26 Aza Asayama, Takahagi 3180004, Japan
关键词
SDS; Sarkosyl; sodium lauroyl glutamate; cell lysis; refolding; neuropathological; POLYACRYLAMIDE-GEL-ELECTROPHORESIS; LAUROYL-L-GLUTAMATE; ESCHERICHIA-COLI; INCLUSION-BODIES; PROTEIN; PURIFICATION; SARKOSYL; TAU; STABILIZATION; DETERGENT;
D O I
10.3390/cimb46010040
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this study, we review the properties of three anionic detergents, sodium dodecyl sulfate (SDS), Sarkosyl, and sodium lauroylglutamate (SLG), as they play a critical role in molecular biology research. SDS is widely used in electrophoresis and cell lysis for proteomics. Sarkosyl and, more frequently, SDS are used for the characterization of neuropathological protein fibrils and the solubilization of proteins. Many amyloid fibrils are resistant to SDS or Sarkosyl to different degrees and, thus, can be readily isolated from detergent-sensitive proteins. SLG is milder than the above two detergents and has been used in the solubilization and refolding of proteins isolated from inclusion bodies. Here, we show that both Sarkosyl and SLG have been used for protein refolding, that the effects of SLG on the native protein structure are weaker for SLG, and that SLG readily dissociates from the native proteins. We propose that SLG may be effective in cell lysis for functional proteomics due to no or weaker binding of SLG to the native proteins.
引用
收藏
页码:621 / 633
页数:13
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