CONTRIBUTION OF SS BONDS TO THE ELASTICITY OF ACTOMYOSIN GEL IN WHICHCOEXISTING TRANSGLUTAMINASE WAS INACTIVATED

The contribution of SS bonds to the elasticity of suwari gel from vari ous actomyosins was investigated, in which the coexisting transglutami nase was inactivated. The actomyosins, whose SH groups were blocked (S H-blocked AM) and unblocked (SH-unblocked AM), were prepared, respecti vely, by shaking the starting actomyosins with and without N-ethylmale imide in 8 M urea. After removal of urea by dialysis, they were measur ed for transglutaminase activity, total SH content, and suwari gel for ming ability. The transglutaminase activity of both the actomyosins be came zero by the above treatment with urea. The suwari gel prepared by setting SH-unblocked AM paste at 40 degrees C for 1 h was considerabl y higher in the breaking force than the gel from the paste of the SH-b locked one. By setting the AM paste, total SH content was somewhat dec reased in the former, but scarcely changed in the latter.