Abstract
The solubility in 8M urea solution (pH 8.5), of carp actomyosin gels formed with or without SH reagents, N-ethylmaleimide and p-chloromercuribenzoate, and the chromatographic patterns of 8M urea soluble fractions of these gels on CPG-10 column were examined in order to prove the participation of SH groups in intermolecular bonding during the gel formation of actomyosin.
It was found that the solubility of actomyosin decreased and the molecular weight of protein molecules increased during the gel formation. These changes were impairted to some extent by adding the SH reagents to actomyosin.
These findings indicate that SH groups are involved in changes to higher molecular weight of protein molecules during the gel formation, and also suggest the formation of SS bonds between protein molecules.
