KMID : 1007519990080020124
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Food Science and Biotechnology 1999 Volume.8 No. 2 p.124 ~ p.127
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Isolation of Metal Binding Plasma Protein by Immobilized Metal Affinity Chromatography
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Choi In-Wook
Chung Soon-Hee
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Abstract
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Porcine plasma proteins were fractionated according to their degree of affinity to ferric or zinc ions by immobilized Fe^(3+) or Zn^(2+) affinity chromatography. The majority of plasma proteins displayed low affinity for immobilized Fe^(3+) and Zn^(2+) sepharose gel. Only one plasma protein showed high affinity to both metals. This protein was a monomer with molecular weight of 81 kDa and mainly composed of glycine, serine, glutamin, or glutamic acid.
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