Abstract
Adsorption isotherms for methyl orange on lysozyme at ionic strengths varying from 0.001 to 0.05, pH 5.5, are sigmoid. Increasing ionic strength shifts the inflection point of such isotherms to higher free anion concentrations. Binding of one methyl orange anion to a lysozyme molecule in 0.05 M acetate, pH 5.5, facilitates adsorption of nine others, with subsequent precipitation of the protein. This co-operative behavior is interpreted on the basis of a previously described theory of interacting hydration effects. The possible biological implications for similar systems are indicated.
Publisher
Canadian Science Publishing
Cited by
5 articles.
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