Abstract
THIS communication shows that the concept of hydro-phobic bonds in interactions of soluble proteins1 can also be applied to water-insoluble fibrous proteins. It has been observed2,3 that lanthionine formation in wool at 65° C with sodium hydrogen carbonate or borate is much faster in mixed solvents than in aqueous solutions. This effect was not explained by the authors. It was also found by Atkinson, Filson and Speakman4,5 that it is more difficult to extend wool fibres in water alone than in saturated aqueous butanol. Now there is evidence that addition of organic solvents will tend to overcome the resistance of the hydrophobic interior of proteins to penetration by the aqueous solvent and thus may increase the reactivity of protein groups located in hydrophobic regions.
Similar content being viewed by others
Article PDF
References
Kauzmann, W., Adv. Protein Chem., 14, 1 (1959).
Zahn, H., and Osterloh, F., Makromol. Chem., 16, 183 (1955).
Zahn, H., and Wiedersich, I., Deutsches Bundespatent, No. 1041216 (1.8.1955).
Filson, A., and Speakman, J. B., J. Soc. Dyers, Col., 74, 762 (1958).
Atkinson, J. C., Filson, A., and Speakman, J. B., Nature, 184, 444 (1959).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
ZAHN, H., GERTHSEN, T. Effect of Propanol–Water Mixtures on the Reactivity of Wool Cystine. Nature 200, 785 (1963). https://doi.org/10.1038/200785a0
Issue Date:
DOI: https://doi.org/10.1038/200785a0
This article is cited by
-
Hydrophobe Wechselwirkungen in Faserproteinen
Kolloid-Zeitschrift und Zeitschrift für Polymere (1964)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.