Liquid chromatography-mass database

Moco S, Bino RJ, Vorst O, Verhoeven HA, de Groot J, van Beek TA, Vervoort J and de Vos CH. 2006. A liquid chromatography-mass spectrometry-based metabolome database for tomato. Plant Physiol 141 (4) 1205—1218. 

Ho YR Hsu PH. Investigating the effects of protein patterns on mieroorganism identification by high-performance liquid chromatography-mass spectrometry and protein database searehes. J Chromatogr A. 2002 976(l-2) 103-11. 

Analytical Chemistry Databases Gas Chromatography Ion Kinetics and Energetics Liquid Chromatography Mass Spectrometry in Forensic Science... 

Figure 5.11. Generic approaches to identify interacting proteins within complexes. The complex is isolated from cells by affinity purification using a tag sequence attached to a protein known to be in the complex. Alternatively, the complex can be immunprecipitated with an antibody to one of the proteins in the complex. The proteins are resolved by polyacrylamide gel electrophoresis, proteolyzed, and the mass of the resulting peptides is determined by mass spectrometry. Alternatively, the proteins can be proteolyzed and the resulting peptides resolved by liquid chromatography. The peptide masses are then determined by mass spectrometry and used for database searching to identify the component proteins.

The main technique used is gas-liquid chromatography (abbreviated GLC or nowadays just GC), which is especially useful when combined with mass spectroscopy (MS) the combination is often referred to as GC-MS. They can provide both quantitative and qualitative information that is very accurate and reliable when compared to known analytical measurements of oils that are stored in databases. 

Figure 4.4. Protein identification by MALDI-TOF. Steps in protein identification by MALDI-TOF are shown. Prior separation by gel or liquid chromatography to a single protein is needed prior to enzymatic digestion with trypsin. Digested peptides are spotted onto a MALDI target with an appropriate matrix that assists desorption of peptides upon activaton by laser. Peaks from the resulting mass spectrum represent peptide ions that can be searched in a database to match a theoretical tryptic digest from known proteins. The more proteins that are matched, the greater the statistical confidence in assignment of a protein identification.

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