Abstract
The effect of dethiothreitol treatment of 6M granidine HCL soluble fractions of carp actomyosin gels on the chromatographic pattern on CPG-10 2000 Å and Bio-Gel A-15 m columns was examined in order to prove the formation of intermolecular SS bonds during the gelformation
It was demonstrated that the polymeric molecules of protein were produced during the gelformation, and the polymeric molecules were depolymerized by treating with dithiothreitol.
On the basis of these findings, it is concluded that polymeric protein molecules in the gelare produced as a result of the rformation of intermolecular SS bnds during heating of actomyosin.