Being solubilized by treatment with 0.01M mercaptoethanol, the ovomucin gel(B) was found in free boundary electrophoresis to contain subunits which were consisted of two components. Changes in the physicochemical properties of all the insoluble ovomucin gel(B) and sol(B) obtained from stored egg white were studied after this treatment.
The fast moving component of the ovomucin gel(B) in free boundary electrophoresis decreased during storage and disappeared completely after 30 days. On the other hand, the fast moving component of the ovomucin sol(B) increased during storage.
The acid mucoprotein concentration of the ovomucin gel(B) in acrylamide gel electro-phoresis decreased and that of the ovomucin soi(B) increased during storage, although the protein pattern did not show significant changes.
The interaction of the ovomucin gel(B) with lysozyme decreased whereas that of the ovomucin sol(B) increased during storage.
By summarizing these results, a model of ovomucin gel structure and a mechanism of egg white thinning were proposed.

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