Abstract

The 7S and 11S fractions of soybean and fababean proteins and also the 12S fraction of rapeseed protein have been analysed for the presence of sulfhydryles groups and disulfide bonds. The measurements have been made with the native proteins and with the same proteins after treatment with guanidine-HCl. The results obtained are presented in terms of distribution of SH-groups and disulfide bridges on the surface and in the interior of the protein molecules, and are discussed in terms of the possible roles played in the polymerization reactions of the various proteins.

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