Immobilized metal affinity chromatography and human serum proteomics

Fengrong Wang, Christyne Chmil, Frank Pierce, Kulothungan Ganapathy, Brooks B Gump, James A. MacKenzie, Yehia Metchref, Kestutis Bendinskas

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)26-33
Number of pages8
JournalJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Volume934
DOIs
StatePublished - Sep 1 2013

Fingerprint

Affinity chromatography
Affinity Chromatography
Proteomics
Metals
Serum
Carrier Proteins
Complement C4b
Proteins
Hemopexin
Apolipoprotein B-100
alpha-Macroglobulins
alpha 1-Antitrypsin
Complement C3
Ceruloplasmin
Prealbumin
Apolipoprotein A-I
Biomarkers
Transferrin
Nickel
Cadmium

Keywords

  • Human serum
  • ICP-MS
  • Immobilized metal affinity chromatography
  • LC-MS/MS
  • Metal binding proteins
  • Proteomics

ASJC Scopus subject areas

  • Biochemistry
  • Analytical Chemistry
  • Cell Biology
  • Clinical Biochemistry

Cite this

Immobilized metal affinity chromatography and human serum proteomics. / Wang, Fengrong; Chmil, Christyne; Pierce, Frank; Ganapathy, Kulothungan; Gump, Brooks B; MacKenzie, James A.; Metchref, Yehia; Bendinskas, Kestutis.

In: Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, Vol. 934, 01.09.2013, p. 26-33.

Research output: Contribution to journalArticle

Wang, Fengrong ; Chmil, Christyne ; Pierce, Frank ; Ganapathy, Kulothungan ; Gump, Brooks B ; MacKenzie, James A. ; Metchref, Yehia ; Bendinskas, Kestutis. / Immobilized metal affinity chromatography and human serum proteomics. In: Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences. 2013 ; Vol. 934. pp. 26-33.
@article{67a02dec38954765950adad6a1386a6a,
title = "Immobilized metal affinity chromatography and human serum proteomics",
abstract = "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.",
keywords = "Human serum, ICP-MS, Immobilized metal affinity chromatography, LC-MS/MS, Metal binding proteins, Proteomics",
author = "Fengrong Wang and Christyne Chmil and Frank Pierce and Kulothungan Ganapathy and Gump, {Brooks B} and MacKenzie, {James A.} and Yehia Metchref and Kestutis Bendinskas",
year = "2013",
month = "9",
day = "1",
doi = "10.1016/j.jchromb.2013.06.032",
language = "English (US)",
volume = "934",
pages = "26--33",
journal = "Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences",
issn = "1570-0232",
publisher = "Elsevier",

}

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

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

UR - http://www.scopus.com/inward/record.url?scp=84881092922&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84881092922&partnerID=8YFLogxK

U2 - 10.1016/j.jchromb.2013.06.032

DO - 10.1016/j.jchromb.2013.06.032

M3 - Article

C2 - 23896426

AN - SCOPUS:84881092922

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

SN - 1570-0232

ER -