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Home >> Biotechnology and Genomics >> Methods and Uses of Genomics and Proteomics Research >> Mass Spectrometry

Mass spectrometry

Mass spectrometric identification of gel-separated proteins is commonly used for further analysis of a proteome. Since whole proteins are difficult to elute and analysed by mass spectrometry, the gel separated proteins are digested into peptides, by one or more sequence specific proteases (e.g. trypsin), so that these trypsinated peptides can then be separated and analysed by mass spectrometry. The different approaches for mass spectrometric analysis of proteins

Differential Display

Much information about the functions of genes and proteins is derived from the analysis of mRNA expression profiles, gene disruption phenotypes, two hybrid interactions, and by subcellular localization of proteins. But these strategies do not give information about the function of proteins at the biochemical level. In biomedical applications, often the objective is to identify proteins that are up-or down-regulated in a disease specific manner, so that these proteins may be used for diagnosis and/or for identification of therapeutic targets. This is achieved by a study of differential display of certain proteins, either by comparative 2-D gel approach or by using protein chips.

 

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