The protein I am purifying needed an elution buffer with 2% Triton X-100. I formulated the elution buffer not keeping the CMC in mind. My goal is to make my protein sample triton free to check its stability and quantify its concentration. Lately, I learnt that micelles can be broken down upon dilution. So, I've diluted my protein sample below triton's CMC and tried concentrating it using Sartorius Vivaspin 5K (PES resin). I loaded 500 ul of diluted sample and was left with 100 ul after concentration using vivaspin. But, this sample gave an abnormal reading of above 3 OD after blanking against the buffer it is in. I presume, triton's interference is causing these discrepant readings.