期刊
PROTEOMICS CLINICAL APPLICATIONS
卷 1, 期 1, 页码 73-88出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/prca.200600276
关键词
albumin-binding proteins; albumin depletion; albuminome; anti-HSA; SEC
资金
- NHLBI NIH HHS [N01HV28180, N01 HV028180] Funding Source: Medline
- DIVISION OF HEART AND VASCULAR DISEASES [N01HV028180] Funding Source: NIH RePORTER
The removal of albumin and other high abundance proteins is a routine first step in the analysis of serum and plasma proteomes. However, as albumin can bind proteins and peptides, there is a universal concern as to how the serum proteome is changed by the removal of albumin. To address this concern, the current study was designed to identify proteins and peptides removed from the serum during albumin depletion; to determine which of these are bound to albumin (rather than copurified) and whether the bound proteins are intact proteins or peptide fragments. Sequential, independent analyses including both anti-albumin antibody (anti-HSA) affinity chromatography and SEC were used to isolate albumin-bound proteins. RP-HPLC and 1-D SD S-PAGE were then used to further separate the proteins prior to identification by MS/MS. Finally, whole protein molecular weight (MW) MS measurements coupled with protein coverage obtained by MS were combined to assess whether the bound proteins were intact or peptide fragments. Combining the results from multiple approaches, 35 proteins, of which 24 are intact, were found to be associated with albumin, and they include both known high and low abundance proteins.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据