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|Title:||The denaturation of protein under high pressure : II. The gelations of ovalbumin solution by pressure and by heat|
|Publisher:||The Physico-Chemical Society of Japan|
|Journal title:||The Review of Physical Chemistry of Japan|
|Abstract:||The gelations of aqueous solution of ovalbumin by heating and by compression have been investigated and compared with the gelation of urea solution of ovalbumin, which had been studied by Huggins et al. and Frensdorff et al. The following results are obtained in both the gelation by heating and that by compression: the optimum pH of gelation is around the isoelectric point, and the lowest protein concentration for gelation rapidly increases with progressing upward or downward from a limited pH range (pH 4-7). The gels near the isoelectric point are highly opaque and synerizing, and easily dissolve when immersed in 0.1N sodium hydroxide. On the other hand, the gels at pH far from the isoelectric point are less opaque and non-synerizing, and do not easily disslove when immersed in 0.1N sodium hydroxide. This tendency is more remarkable in thermal gel than in pressure gel. These results indicate that the coarse network by the secondary bonds holds the gel formed from the solution near the isoelectric point, and the fine network by chemical bonds holds the gel formed from the solution near neutral pH. The formation of the inhomogeneous and coarse network by the secondary bonds is most favorable in the pressure gelation, and next in the thermal gelation, but it is not favorable in the gelation of urea solution of ovalbumin.|
|Appears in Collections:||Vol.33 No.2|
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