Abstract
1. Solutions of proteins were subjected to gentle agitation in the presence of small quantities of decane containing different alcohols. 2. Some of the protein was lost from solution and adsorbed on the surface of the emulsion formed; at the same time some decane was bound to the protein remaining in solution. 3. Comparison of these results with those obtained with pure decane suggests that a mixed film of protein+alcohol is formed on the surface of the emulsion. 4. If the concentration of alcohol in decane is increased the amount of protein adsorbed on the emulsion is decreased. This phenomenon was used to compare the effect of different alcohols in disrupting the hydrophobic interactions between proteins and hydrocarbons.
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Selected References
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