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Liquid Chromatography In Clinical Analysis pp 323–353Cite as

Proteins

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Part of the book series: Biological Methods ((BM))

Abstract

Because of the complexity of cellular material and body fluids, it is seldom possible to analyze a natural product directly. Qualitative and quantitative analyses must often be preceded by some purification step that separates the molecular species being examined from interfering materials. In the case of proteins, column liquid chromatography has been used extensively for these fractionations. With the advent of gel permeation, cation exchange, anion exchange, hydrophobic, and affinity chromatography, it became possible to resolve proteins through their fundamental properties of size, charge, hydrophobicity, and biological affinity. The chromatographic separations used in the early isolation and characterization of many proteins later became analytical tools in their routine analysis. Unfortunately, these inherently simple and versatile column chromatographic techniques introduced in the 50s and 60s have a severe limitation in routine analysis-separation time. It is common to encounter 1–24 h separation times with the classical gel-type supports.

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Author information

Authors and Affiliations

  1. Department of Biochemistry, Purdue University, West Lafayette, Indiana

    Fred E. Regnier & Karen M. Gooding

Authors
  1. Fred E. Regnier
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  2. Karen M. Gooding
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Editor information

Editors and Affiliations

  1. University of California School of Medicine, San Francisco, California

    Pokar M. Kabra  & Laurence J. Marton  & 

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© 1981 The Humana Press, Inc.

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Regnier, F.E., Gooding, K.M. (1981). Proteins. In: Kabra, P.M., Marton, L.J. (eds) Liquid Chromatography In Clinical Analysis. Biological Methods. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60327-404-3_14

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  • DOI: https://doi.org/10.1007/978-1-60327-404-3_14

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-0-89603-026-8

  • Online ISBN: 978-1-60327-404-3

  • eBook Packages: Springer Book Archive

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