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.
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