Plasma/serum samples pose specific challenges for proteomic profiling. Complexity of these samples consisting of more than 15,000 proteins (3020 core proteins) is one reason, however this is further complicated by a dynamic range of concentrations of twelve orders of magnitude. The latter property of serum/plasma samples requires elimination of highly abundant proteins to enable quality identification and quantification of low abundant proteins. Removal of most abundant proteins such as serum albumin is accomplished by affinity (also immunoaffinity) techniques, however, protein-protein interactions, whether specific or not, will cause removal of some proteins that can be found in albuminome, a fraction of affinity removed serum albumin. Affinity depletion techniques are discussed together with such aspects as reproducibility and quality control. A list of human plasma proteins co-immunodepleted with albumin is provided.
|Original language||English (US)|
|Title of host publication||Proteomic Profiling and Analytical Chemistry|
|Subtitle of host publication||The Crossroads: Second Edition|
|Number of pages||14|
|State||Published - Mar 22 2016|
- Proteomic sample preparation
ASJC Scopus subject areas