How does mass spectrometry achieve quantification?
Mass Spectrometry (MS) is an analytical technique used to measure the mass-to-charge ratio (m/z) of ions. In mass spectrometry analysis, molecules in the sample are converted into ions with positive or negative charges, which are then separated and detected by the electromagnetic field in the mass spectrometer. Mass spectrometry can provide information about the mass, structure, and composition of molecules. Through mass spectrometry, qualitative and quantitative analysis of various components in a sample can be achieved.
The principle of achieving quantification in mass spectrometry is mainly based on the relationship between the signal intensity of ions and their concentration. In mass spectrometry, the signal intensity (peak height or peak area) of each ion is proportional to its concentration in the sample. Therefore, by comparing the signal intensity of the target ions with the signal intensity of standard ions with known concentrations, quantitative analysis of the target components can be achieved.
Common quantitative methods based on mass spectrometry include:
1. Label-based methods:
By introducing stable isotope labels into protein samples, proteins from different experimental conditions or organisms can be distinguished. Common labeling methods include Isotope-Coded Affinity Tags (ICAT),Stable Isotope Labeling by/with Amino acids in Cell culture(SILAC),Isobaric Tags for Relative and Absolute Quantitation(iTRAQ), andTandem Mass Tag(TMT), etc.
Quantification is achieved by directly comparing the relative abundance of the same protein in mass spectrometry profiles. This method does not require stable isotope labeling and is suitable for a wider range of sample types. Common label-free methods include ion counting and feature extraction methods.
By using methods such as Selected Reaction Monitoring (SRM), Multiple Reaction Monitoring (MRM), or Parallel Reaction Monitoring (PRM), the abundance of specific proteins can be measured in a targeted manner. These methods usually have high sensitivity and accuracy, making them suitable for verifying key findings in large-scale proteomics studies.
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