Loss of filament-forming ability of myosin by non-enzymatic glycosylation and its molecular mechanism.

Carp and scallop myosin and their subfragments (S-1 and rod) were reacted with glucose to investigate the effect of non-enzymatic glycosylation on the functionality of myosin. The filament-forming ability of the myosin rod diminished with the progress of non-enzymatic glycosylation and myosin became soluble in 0.1 M NaCl. The inhibition of the self-assembly of myosin molecules occurred chemically as a result of the increase in negative charge repulsion among myosin molecules and, further, physically as a result of the introduction of the glycosyl units into the surface of the rod region.