HEAT-INDUCED GELATION OF MYOSINS SUBFRAGMENTS FROM CHICKEN LEG AND BREAST MUSCLES AT HIGH IONIC-STRENGTH AND LOW PH

Heat-induced gelation was studied to examine the reason for marked differences in gel strength of myosins at 0.6M KCl and pH 5-6. When leg myosin (L-myosin) or L-myosin tail subfragment was mixed with breast myosin (B-myosin) or B-myosin tail subfragment, rigidity of the mixture gel was higher than the sum of rigidities of the component gels. Difference in strength of heat-induced gel between L- and B-myosin seemed to be caused by differences in filament-forming ability and in gel-forming ability of head and tail segments of both kinds of myosins.