Conformation Changes and Subsequent Gelation of Conalbumin by a Thiol Reagent(Biological Chemistry)

概要

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Thiol reagents have been shown to induce the gelation of conalbumin [M. Hirose, H. Oe and E. Doi, Agric. Biol. Chem., 50,59 (1986)]. The gelation mechanisms were investigated in relation to the structure of this protein. Following the addition of 2-mercaptoethanol, the sulfhydryl groups of conalbumin increased almost linearly during the first 50min of incubation. The relative hydrophobicity measured by fluorescent dyes increased concomitantly with increases in the sulfhydryl groups. The circular dichroism spectra revealed that the thiol reagent induces some changes in the tertiary structure but no prominent alterations in the secondary structure. The transmission electron microscopic study showed that at 20 min of incubation conalbumin formed rod-like structures and that at 32min of incubation these structures produced branched aggregates. The SDS-polyacrylamide gel electrophoresis indicated that intermolecular covalent interactions are not involved in the formation of conalbumin gel.
社団法人日本農芸化学会の論文
1986-10-23