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Loss of filament‐forming ability of myosin by non‐enzymatic glycosylation and its molecular mechanism
Author(s) -
Katayama Shigeru,
Haga Yoshiaki,
Saeki Hiroki
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.08.029
Subject(s) - myosin , glycosylation , chemistry , protein filament , biophysics , enzyme , carp , biochemistry , biology , fish <actinopterygii> , fishery
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.