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.
Katayama
Shigeru
S
Graduate School of Fisheries Sciences, Hokkaido University, Hakodate 041-8611, Japan.
Haga
Yoshiaki
Y
Saeki
Hiroki
H
D000818:Animals; D002347:Carps / Q000378:metabolism; D005947:Glucose / Q000378:metabolism*; D006031:Glycosylation; D006863:Hydrogen-Ion Concentration; D008974:Mollusca / Q000737:chemistry; D009210:Myofibrils / Q000737:chemistry / Q000378:metabolism; D015879:Myosin Subfragments / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D009218:Myosins / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D017433:Protein Structure, Secondary; D012995:Solubility; D013696:Temperature
D015879:Myosin Subfragments; D009218:Myosins; D005947:Glucose