TY - JOUR
T1 - Immobilized metal affinity chromatography and human serum proteomics
AU - Wang, Fengrong
AU - Chmil, Christyne
AU - Pierce, Frank
AU - Ganapathy, Kulothungan
AU - Gump, Brooks B.
AU - MacKenzie, James A.
AU - Metchref, Yehia
AU - Bendinskas, Kestutis
N1 - Funding Information:
Authors thank Dr. Paul Tomascak, Associate Professor of Geology & Geochemistry of SUNY-Oswego for his ICP-MS analysis of our samples. We thank SUNY-Oswego for the financial support of this work. The funding source had no involvement in the study design nor in the collection, analysis, or interpretation of data.
PY - 2013/9/1
Y1 - 2013/9/1
N2 - Metal-binding proteins have a pivotal role in normal and diseased states. We used metal affinity chromatography to enrich a fraction of human serum proteins on immobilized columns loaded with cadmium, nickel, zinc, copper, or lead in bis-Tris saline and these proteins were identified using LC-MS/MS. Tens of enriched proteins were identified and we here present the 20 most abundant for binding each metal. The binding of various proteins (complement C3, alpha-2-macroglobulin, serum albumin, apolipoprotein B-100, complement component 4B preproprotein, apolipoprotein A-I, serotransferrin, alpha-1-antitrypsin, ceruloplasmin, 47. kDa protein, uncharacterized protein DKFZp686P15220, transthyretin, hemopexin, inter-alpha-trypsin inhibitor heavy chain H2, and histidine-rich glycoprotein) to different metals using immobilized metal affinity chromatography was compared to the literature. Although many metal-binding properties of these proteins have been confirmed, new metal-binding proteins have also been identified. The metal array use in the proteomic biomarker search technologies gives this data particular importance.
AB - Metal-binding proteins have a pivotal role in normal and diseased states. We used metal affinity chromatography to enrich a fraction of human serum proteins on immobilized columns loaded with cadmium, nickel, zinc, copper, or lead in bis-Tris saline and these proteins were identified using LC-MS/MS. Tens of enriched proteins were identified and we here present the 20 most abundant for binding each metal. The binding of various proteins (complement C3, alpha-2-macroglobulin, serum albumin, apolipoprotein B-100, complement component 4B preproprotein, apolipoprotein A-I, serotransferrin, alpha-1-antitrypsin, ceruloplasmin, 47. kDa protein, uncharacterized protein DKFZp686P15220, transthyretin, hemopexin, inter-alpha-trypsin inhibitor heavy chain H2, and histidine-rich glycoprotein) to different metals using immobilized metal affinity chromatography was compared to the literature. Although many metal-binding properties of these proteins have been confirmed, new metal-binding proteins have also been identified. The metal array use in the proteomic biomarker search technologies gives this data particular importance.
KW - Human serum
KW - ICP-MS
KW - Immobilized metal affinity chromatography
KW - LC-MS/MS
KW - Metal binding proteins
KW - Proteomics
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U2 - 10.1016/j.jchromb.2013.06.032
DO - 10.1016/j.jchromb.2013.06.032
M3 - Article
C2 - 23896426
AN - SCOPUS:84881092922
SN - 1570-0232
VL - 934
SP - 26
EP - 33
JO - Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
JF - Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
ER -