1990 Volume 37 Issue 6 Pages 446-453
Myosin B, myosin and actin were polymerized and gelled by Ca2+-independent transglutaminase (B.T.G.) derived from a microorganism (Streptoverticillium). The concentration of B.T.G. required for gelation of myosin B was lower than that for myosin and actin. On SDS-PAGE of myosin B treated with B.T.G., the monomeric myosin heavy chain decreased markedly with increasing amount of B.T.G. and a polymer fraction increased. Analysis of actin by SDS-PAGE indicated that actin was also polymerized. The small amount of B.T.G. increased the turbidity of myosin B induced by heating of linearly increasing rate of 2°C/min, suggesting that myosin B suspension with B.T.G. formed a finer network structure of heat-induced gel than that of myosin B alone. When the myosin B solution with B.T.G. was heated and then the heat induced gel centrifuged; tropomyosin and troponin-T were not freed from the sediment. These results suggest that the regulatory proteins play some role in the heat-induced gelation of this system.
