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Size-exclusion chromatographic behavior of bovine serum albumin in uni-uni valent ions solutions

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Summary

Molecular interaction between uni-uni valent ions and bovine serum albumin was investigated by size-exclusion chromatography. Elution profiles are first presented for salt and protein solutions as samples with water as the mobile phase; then for water and protein as samples with salt solutions as the mobile phase. The results suggest the existence of a dynamic equilibrium between the salt ions and the protein ions as reactants and the ion-pair (salt-protein) complex as a product.

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Authors and Affiliations

  1. Department of Chemistry, St. John's University, 11439, Jamaica, New York, (USA)

    S. F. Sun

  2. Department of Industrial Pharmacy, College of Pharmacy and Allied Health, St. John's University, 11439, Jamaica, New York, (USA)

    S. Del Terzo & R. A. Nash

Authors
  1. S. F. Sun
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  2. S. Del Terzo
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  3. R. A. Nash
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Sun, S.F., Del Terzo, S. & Nash, R.A. Size-exclusion chromatographic behavior of bovine serum albumin in uni-uni valent ions solutions. Chromatographia 20, 303–307 (1985). https://doi.org/10.1007/BF02310387

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  • DOI: https://doi.org/10.1007/BF02310387

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