Abstract
Gel was obtained when alkaline dope solutions of the 7S and 11S globulins (8% protein concentration) prepared at pH above 11 were dialyzed against phosphate buffer, pH 7.6, µ= 0.3. To make clear the mechanism of gelation, the relationship between changes in viscosity and aggregation phenomena of the neutralized dope solutions was investigated by means of viscosity measurement, disc electrophoresis and gel filtration, comparing the 7S and 11S fractions. In conclusion, it is revealed that the gel is constituted with macromolecule aggregates, and to form the aggregates which are suitable for gelation, all of the following conditions must be satisfied at least : 1); Unfolding and dissociation into subunits once (above pH 11), 2); High ionic strength in the media (µ=0.3), 3); Formation of hydrogen, hydrophobic and disulfide bonds, 4); High protein concentration (above 8%).
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