Is the Sample Preparation for Protein Detection Using MALDI-TOF and QE Mass Spectrometry the Same
MALDI-TOF (Matrix-Assisted Laser Desorption/Ionization Time-of-Flight) mass spectrometry and QE (Quadrupole-Orbitrap) mass spectrometry are two different mass spectrometry techniques, and their pretreatment steps in protein detection have some differences. The pretreatment for MALDI-TOF tends to involve directly mixing the sample with a matrix to form crystals, whereas the QE mass spectrometry pretreatment focuses more on liquid chromatography separation and ionization of proteins or peptides.
MALDI-TOF Mass Spectrometry Pretreatment
1. Sample Preparation
This involves mixing the protein sample with a matrix. The matrix plays a role in assisting the protein sample in absorbing laser energy and achieving desorption/ionization.
2. Spotting
The mixture is applied onto a MALDI plate to form spots.
3. Crystallization
The co-crystallization of the matrix and protein is a crucial step, which is essential for efficient laser desorption/ionization.
QE Mass Spectrometry Pretreatment
1. Sample Preparation
Typically involves protein digestion, such as trypsin treatment, to generate peptides, which are then used for mass spectrometry analysis.
2. Liquid Chromatography Separation
Peptides usually need to be separated by liquid chromatography (LC) to reduce sample complexity.
3. Electrospray Ionization
QE mass spectrometry commonly employs electrospray ionization (ESI) as the ionization source, which requires the sample to be introduced in liquid form.
MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.
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