Comparison of different transition metal ions for immobilized metal affinity chromatography of selenoprotein P from human plasma

U Sidenius; O Farver; O Jøns; Bente Gammelgaard

Comparison of different transition metal ions for immobilized metal affinity chromatography of selenoprotein P from human plasma

U Sidenius, O Farver, O Jøns, Bente Gammelgaard

23 Citationer (Scopus)

Abstract

Cu2+, Ni2+, Zn2+, Co2+ and Cd2+ were evaluated in metal ion affinity chromatography for enrichment of selenoprotein P, and immobilized Co2+ affinity chromatography was found to be the most selective chromatographic method. The chromatography was performed by fast protein liquid chromatography and the fractionation was followed by analysis of the collected fractions for selenium by inductively coupled plasma mass spectrometry. By the combination of immobilized Co2+ affinity chromatography and heparin affinity chromatography a simple method was developed yielding a 14,800-fold enrichment of selenoprotein P. The purity of the protein was determined by SDS-PAGE and by sequencing from polyvinylidene difluoride blots of SDS-PAGE gels.

Originalsprog	Engelsk
Tidsskrift	Journal of Chromatography B: Biomedical Sciences and Applications
Vol/bind	735
Udgave nummer	1
Sider (fra-til)	85-91
Antal sider	7
ISSN	1387-2273
Status	Udgivet - 1999

Citationsformater

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title = "Comparison of different transition metal ions for immobilized metal affinity chromatography of selenoprotein P from human plasma",

abstract = "Cu2+, Ni2+, Zn2+, Co2+ and Cd2+ were evaluated in metal ion affinity chromatography for enrichment of selenoprotein P, and immobilized Co2+ affinity chromatography was found to be the most selective chromatographic method. The chromatography was performed by fast protein liquid chromatography and the fractionation was followed by analysis of the collected fractions for selenium by inductively coupled plasma mass spectrometry. By the combination of immobilized Co2+ affinity chromatography and heparin affinity chromatography a simple method was developed yielding a 14,800-fold enrichment of selenoprotein P. The purity of the protein was determined by SDS-PAGE and by sequencing from polyvinylidene difluoride blots of SDS-PAGE gels.",

keywords = "Affinity Labels, Amino Acid Sequence, Cadmium, Chromatography, Affinity, Cobalt, Copper, Electrophoresis, Polyacrylamide Gel, Humans, Metals, Molecular Weight, Nickel, Proteins, Selenoprotein P, Selenoproteins, Sepharose, Zinc",

author = "U Sidenius and O Farver and O J{\o}ns and Bente Gammelgaard",

year = "1999",

language = "English",

volume = "735",

pages = "85--91",

journal = "Journal of Chromatography B: Biomedical Sciences and Applications",

issn = "1387-2273",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

T1 - Comparison of different transition metal ions for immobilized metal affinity chromatography of selenoprotein P from human plasma

AU - Sidenius, U

AU - Farver, O

AU - Jøns, O

AU - Gammelgaard, Bente

PY - 1999

Y1 - 1999

N2 - Cu2+, Ni2+, Zn2+, Co2+ and Cd2+ were evaluated in metal ion affinity chromatography for enrichment of selenoprotein P, and immobilized Co2+ affinity chromatography was found to be the most selective chromatographic method. The chromatography was performed by fast protein liquid chromatography and the fractionation was followed by analysis of the collected fractions for selenium by inductively coupled plasma mass spectrometry. By the combination of immobilized Co2+ affinity chromatography and heparin affinity chromatography a simple method was developed yielding a 14,800-fold enrichment of selenoprotein P. The purity of the protein was determined by SDS-PAGE and by sequencing from polyvinylidene difluoride blots of SDS-PAGE gels.

AB - Cu2+, Ni2+, Zn2+, Co2+ and Cd2+ were evaluated in metal ion affinity chromatography for enrichment of selenoprotein P, and immobilized Co2+ affinity chromatography was found to be the most selective chromatographic method. The chromatography was performed by fast protein liquid chromatography and the fractionation was followed by analysis of the collected fractions for selenium by inductively coupled plasma mass spectrometry. By the combination of immobilized Co2+ affinity chromatography and heparin affinity chromatography a simple method was developed yielding a 14,800-fold enrichment of selenoprotein P. The purity of the protein was determined by SDS-PAGE and by sequencing from polyvinylidene difluoride blots of SDS-PAGE gels.

KW - Affinity Labels

KW - Amino Acid Sequence

KW - Cadmium

KW - Chromatography, Affinity

KW - Cobalt

KW - Copper

KW - Electrophoresis, Polyacrylamide Gel

KW - Humans

KW - Metals

KW - Molecular Weight

KW - Nickel

KW - Proteins

KW - Selenoprotein P

KW - Selenoproteins

KW - Sepharose

KW - Zinc

M3 - Journal article

C2 - 10630893

SN - 1387-2273

VL - 735

SP - 85

EP - 91

JO - Journal of Chromatography B: Biomedical Sciences and Applications

JF - Journal of Chromatography B: Biomedical Sciences and Applications

IS - 1

ER -

Comparison of different transition metal ions for immobilized metal affinity chromatography of selenoprotein P from human plasma

Abstract

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