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The strength formation process of the mixture is analyzed by performing a laboratory test to establish the dynamic stability estimation model.
Proteins are digested with a protease, and the peptide mixture is analyzed by liquid chromatography-mass spectrometry (LC/MS) and liquid chromatography with tandem mass spectrometry (LC/MS/MS); the relative protein abundance is determined by chromatographic peak intensity measurement.
Secondly, the profiles could be used to guide glycoproteomics analyses where tryptic peptides are extracted, glycopeptides are enriched, and the mixture is analyzed by LC-MS/MS.
In a typical "bottom-up" approach, also known as the shotgun proteomics strategy, the enzyme-digested protein mixture is analyzed using single- or multi-dimensional chromatography coupled with tandem mass spectrometry [ 1, 2].
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The mixture was analyzed by chiral HPLC before adding lipase.
This mixture was analyzed by HPLC at different time points.
The penetration depth for each mixture was analyzed.
To calculate a conversion yield, the reaction mixture was analyzed using RP-HPLC.
Evaporation of a single drop injected in a stream of gas solid mixture was analyzed first.
After at least 2 h at room temperature, the reaction mixture was analyzed by LC-ESI-MS/MS and GC–MS, respectively.
The amount of HCPT in the sonicated mixture was analyzed by fluorescence spectroscopy (excitation at 382 nm).
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