Polymerization of beef actomyosin was induced by addition of transglut
aminase. The relative intensity analyzed by densitometry after sodium
dodecyl sulfate polyacrylamide gel electrophoresis indicated that band
s containing the polymerized myosin increased from 10.1 +/- 2.2% to 20
.7 +/- 3.5% while the myosin monomer band decreased from 20.9 +/- 3.4%
to 13.0 +/- 2.7% as the reaction time extended from 10 to 120 min at
35-degrees-C. Polymerization of actomyosin induced by transglutaminase
resulted in gelation of the actomyosin that was visualized by confoca
l laser scanning microscopy.