Cationic and anionic detergent buffers in sequence yield high-quality genomic DNA from diverse plant species

Krishnan, Saranya; Sasi, Shina; Kodakkattumannil, Preshobha; Al Senaani, Salima; Lekshmi, Geetha; Kottackal, Martin; Amiri, Khaled M.A.

doi:10.1016/j.ab.2023.115372

Cited by 1 publication

(1 citation statement)

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Detergents are one of the most widely used reagents in molecular biology research [1][2][3]. Their use includes but is not limited to cell lysis, electrophoresis, protein refolding, and the suppression of macromolecular surface adsorption or aggregation, i.e., a manipulation of macromolecular solutions [4].…”

Section: Introductionmentioning

confidence: 99%

Sodium Dodecyl Sulfate Analogs as a Potential Molecular Biology Reagent

Arakawa,

Niikura,

Kita

et al. 2024

CIMB

View full text Add to dashboard Cite

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.

show abstract