Effect of Salts on the Thiol-dependent Gelation of Bovine Serum Albumin(Food & Nutrition)

概要

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A previous report has shown that the thio-dependent gelation of bovine serum albumin was strongly inhibited by high concentrations of salts. The inhibition mechanism was investigated in relation to the conformation and disulfide cleavage of the protein. The effects on the thiol-dependent disulfide cleavage of the protein varied with the salt species, especially with the anion species. The circular dichroism spectra and difference UV-spectra showed that anions induced some conformational changes in the tertiary structure, but not in the secondary structure. With regard to a chaotropic anion, perchlorate, this conformational change was closely correlated with the inhibition of gelation and disulfide reduction. In contrast, a lyotropic anion such as sulfate inhibited the gelation at a higher concentration than the effect on disulfide reduction. Thus, we conclude that there are two inhibition sites for the thiol-dependent gelation of BSA. One involves the reductive cleavage of disulfide bonds, and the other probably concerns intermolecular interaction of the disulfide-reduced protein.
社団法人日本農芸化学会の論文
1991-08-23