 |
|
| App. Note 344: Top-Down Analysis of the Low Molecular Weight Human Plasma Proteome Using Hybrid Ion Trap-Fourier Transform Mass Spectrometry. |
| This application note demonstrates the effectiveness of the LTQ FT, to detect and identify both intact LMW plasma proteins and peptides belonging to the plasma peptidome in an enzyme-free protocol. |
| Characterization of the plasma proteome is a daunting analytical task due to the large number of proteins thought to be present and the extremely large dynamic range of their concentrations. Historically, several different analytical approaches have been incorporated to identify proteins belonging to the low molecular weight (LMW) plasma proteome, including various enrichment schemes and numerous bottom-up mass spectrometric analyses. For bottom-up analysis, the protein s digested with an enzyme to give a mixture of peptides which are identi- fied from database analysis of their CID fragmentation spectra to lead to the identity of the source protein. By contrast, top-down analysis enables the study of the intact protein, allowing identification, primary structure determination and localization of post-translational modifications (PTMs) directly at the protein level, without the need for enzymatic digests. In this report, a novel top-down approach is used for characterizing the LMW proteome and plasma peptidome using the LTQ FT, a hybrid linear ion trap-Fourier transform mass spectrometer.
To read the complete application note, please download the PDF file on the left side of this page.
|
|
|
Products used for this Application |
|
|
|
| |
| |
|
|
|
0 Items 