As a known non-ionic, -denaturing detergent and emulsifier, Triton™ X-100 is often used in various biochemical studies including in the isolation of membrane-protein complexes for solubilizing membrane proteins, in the process of periplasmic protein extraction as a component of the lysis buffer, in both indirect immunofluorescence staining and flow cytometry as a permeabilization reagent, etc. It has been shown that the diluted solution of Triton™ X-100 with the optimal pH range of 6.0-8.0 has a significant absorption of UV light. In the present project, we show that the absorption spectrum of Triton™ X-100, when dissolved in 1X phosphate-buffered saline, is similar to that of α-synuclein, as a representative of those proteins lack tryptophan but contain tyrosine as their main UV absorber. These results show that whenever the use of Triton™ X-100 for extracting membrane and periplasmic proteins is inevitable, scavenging it before the characterization of the proteins by UV-Vis spectroscopy, especially the determination of their concentration using Beer-Lambert Law, would be necessary.
Nedaei, H., & Saboury, A. A. (2021). Triton™ X-100 Behaves Similarly to Tyrosine-Containing and Tryptophan-Free Proteins in UV-Vis Spectroscopy. Physical Chemistry Research, 9(2), 253-260. doi: 10.22036/pcr.2021.241057.1797
MLA
Hadi Nedaei; Ali Akbar Saboury. "Triton™ X-100 Behaves Similarly to Tyrosine-Containing and Tryptophan-Free Proteins in UV-Vis Spectroscopy". Physical Chemistry Research, 9, 2, 2021, 253-260. doi: 10.22036/pcr.2021.241057.1797
HARVARD
Nedaei, H., Saboury, A. A. (2021). 'Triton™ X-100 Behaves Similarly to Tyrosine-Containing and Tryptophan-Free Proteins in UV-Vis Spectroscopy', Physical Chemistry Research, 9(2), pp. 253-260. doi: 10.22036/pcr.2021.241057.1797
VANCOUVER
Nedaei, H., Saboury, A. A. Triton™ X-100 Behaves Similarly to Tyrosine-Containing and Tryptophan-Free Proteins in UV-Vis Spectroscopy. Physical Chemistry Research, 2021; 9(2): 253-260. doi: 10.22036/pcr.2021.241057.1797