Macrophage iron content was determined by using inductively coupled plasma mass spectrometry.

Several recurrent problems have always hindered mono-dimensional liquid chromatography- mass spectrometry proteomic analyses.

The tags require novel methods of quantification analysis using tandem mass spectrometry.

The nucleotide sequences of the extension products were determined by mass spectrometry.

We used one- and two-dimensional liquid chromatography combined with data-independent mass spectrometry.

Tacrolimus concentrations were measured using validated turbulent flow chromatography-tandem mass spectrometry methods.

Its presence was confirmed by high performance liquid chromatography-electrospray ionization-tandem mass spectrometry.

Structural characterization was performed by mass spectrometry and nuclear magnetic resonance analyses.

All samples were analyzed using Western blots and targeted tandem mass spectrometry.

Following biotin-affinity capture, the biotinylated proteins can be identified using mass spectrometry.

These isomeric components were identified by collision analysis and tandem mass spectrometry.

Holmium accumulation in organs was measured using inductively coupled plasma mass spectrometry.

SUMOylation target proteins were elucidated using mass spectrometry and proximity ligation assay.

Modern mass spectrometry now permits genome-scale and quantitative measurements of biological proteomes.

We do a base extraction followed by liquid chromatography and mass spectrometry.

It then uses an advanced mass spectrometry technique to identify the sample.