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The pH Stability Region of Insoluble Proteins

Nature volume 127, pages 665–666 (1931)Cite this article

Abstract

BY means of the ultracentrifugal method developed in his laboratory, Svedberg 1 has measured the stability of a number of soluble proteins as a function of the pH of the environment. Each of the monodisperse proteins was found to have a fairly wide pH-stability region which included the isoelectric point. By means of a totally different technique, we have recently been able to show that insoluble proteins, such as wool keratin, are no exception to the above rule. The method, which we believe to have a general application, took its origin in the observation that the resistance of wool fibres to extension is far less in acid solution than in distilled water. This, and the well known ease of extension of fibres in alkaline solution, give a method for studying the stability of the keratin in various media. FIG. 1.

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References

  1. Svedberg, "General Discussion on Colloid Science applied to Biology". Trans. Faraday Soc., p. 740 ; 1930.

  2. Speakman, J. Soc. Dyers and Colourists, 25, 172 ; 1925.

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  3. Svedberg, loc. cit., p. 741.

  4. Speakman, Proc. Roy. Soc, 103, B, 389 ; 1928.

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  5. Meyer and Mark, "Der Aufbau der Hochpolymeren Organischen Naturstoffe". Leipzig, 1930, p. 224.

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Authors and Affiliations

  1. Textile Chemistry Laboratory, University, Leeds

    J. B. SPEAKMAN & MERCIA C. HIRST

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  1. J. B. SPEAKMAN
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  2. MERCIA C. HIRST
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SPEAKMAN, J., HIRST, M. The pH Stability Region of Insoluble Proteins. Nature 127, 665–666 (1931). https://doi.org/10.1038/127665a0

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