I am trying to measure small molecule fluorescence in acidified ethanol brain lysate and need to remove protein, which is peaking around where my compound signal should be. Would a MWCO filtration tube be a good method for protein removal? I need at least 50uL final volume per sample to use in our machine.
Mrs/Miss Cavalier,
Any analyte, despite its molecular weight and the complexity of the matrix can be quantified exactly by means of mass spectrometry within the frameworok of our innovative strochastic dynamic method and new formulas for treatment of MS experimental variables.
Also, our method is capable of providing exact 3D information of the analytes.
Please, consider the reference section to discussion [A].
[A] [https://www.researchgate.net/post/How_can_we_detect_VOCs_in_exhaled_breath_sample_using_ISQ_7000_single_quadrupole_GC-MS_system]
The methods of mass spectrometry provide imaging technique, as well.
Obviously enough, they are methods of choice for the purpose of your analysis.
Toward, the accuracy of the Fs data, please consider some detain on discussion [B].
[B]
[https://www.researchgate.net/post/Sensitivity_Coefficient_in_Uncertainty_Calculations_for_HPLC_assay_method_UV_assay_methods_and_pH_measurement]
Running the sample through a centrifugal ultrafiltration device, or as you put it a MWCO filtration tube, will remove proteins that are too large to pass through the filter. Make sure you check that the membrane type is compatible with the solvent. You should also check that the compound does not get stuck on the filter.
You should also think about whether other low molecular weight substances in the extract may also be interfering in your measurement. If so, you will have to add some sort of separation step to the analysis, such as HPLC. To check for this, just prepare a sample without the small molecule.
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