TY - JOUR ID - 125907 TI - Triton™ X-100 Behaves Similarly to Tyrosine-Containing and Tryptophan-Free Proteins in UV-Vis Spectroscopy JO - Physical Chemistry Research JA - PCR LA - en SN - 2322-5521 AU - Nedaei, Hadi AU - Saboury, Ali Akbar AD - Department of Biophysics, Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran 14176-14335, Iran Y1 - 2021 PY - 2021 VL - 9 IS - 2 SP - 253 EP - 260 KW - Triton™ X-100 KW - Detergent KW - Membrane proteins KW - Periplasmic proteins KW - α-Synuclein KW - UV-Vis spectroscopy KW - Beer-Lambert law DO - 10.22036/pcr.2021.241057.1797 N2 - 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. UR - https://www.physchemres.org/article_125907.html L1 - https://www.physchemres.org/article_125907_8c96286a50800f99fb4ea1f0ca2cc64f.pdf ER -