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Hydrophobic Adsorption Chromatography of Proteins

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Methods of Protein Separation

Part of the book series: Biological Separations ((BIOSEP))

Abstract

Until relatively recently, only one general protein property, i.e., electrical charge in the case of ion exchange adsorbents, was wittingly employed as a parameter for nonspecific adsorption chromatography of proteins. One of the reasons for the delay of investigations of possible hydrophobic effects probably was the assumption that hydrophobic groups of proteins generally are situated in the interior of the native protein molecule and thus are inaccessible. The occurrence of external hydrophobic groups was looked upon as relatively rare. However, recent observations (Klotz, 1970) indicate that the hydrophobic amino acid side chains, including the largest ones such as those of phenylalanine and tryptophan, occur much more frequently on the surface of native protein molecules than had been assumed. These findings are in accord with the “extremely wide range of processes in which hydrophobic bonding plays a critical role” (Dunn andHansch, 1974) and with the observation that in the presence of high salt concentrations many proteins are bound by adsorbents carrying hydrophobic groups (Hofstee, 1973a; Porath et al., 1973; Hjertén, 1973).

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Authors and Affiliations

  1. Biochemistry Division, Palo Alto Medical Research Foundation, Palo Alto, California, 94301, USA

    B. H. J. Hofstee

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  1. B. H. J. Hofstee
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  1. Massachusetts Institute of Techonology, Cambridge, Massachusetts, USA

    Nicholas Catsimpoolas

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Hofstee, B.H.J. (1976). Hydrophobic Adsorption Chromatography of Proteins. In: Catsimpoolas, N. (eds) Methods of Protein Separation. Biological Separations. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-9984-1_7

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  • DOI: https://doi.org/10.1007/978-1-4684-9984-1_7

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