Abstract
Myosin rod regions prepared from carp Cyprinus carpio dorsal muscle and scallop Pecten yessoensis striated adductor muscle were non-enzymatically reacted with glucose (glycation), and the changes in the filament-forming ability and the size distribution of the rod filaments during glycation were examined to discuss the molecular mechanism of the water solubilization of myosin molecules under physiological conditions. Both myosin rods became solubilized in 0.1 M NaCl (pH 7.5), and their filament-forming ability was weakened with the progress of glycation. The size of the insoluble filaments of the myosin rods was diminished with an increase in the solubility under physiological conditions, and glycated myosin rods finally existed as monomers in 0.1 M NaCl (pH 7.5). These results supported the hypothesis that the water solubilization of myosin by glycation was caused by the loss of the filament-forming ability of myosin molecules. Water solubilization seemed to occur through the same molecular mechanism regardless of the species, whereas the scallop myosin rods required a much larger number of lysine residues reacted with glucose to collapse the insoluble filaments, in contrast to the carp myosin rods.
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An erratum to this article is available at http://dx.doi.org/10.1111/j.1444-2906.2007.01424.x.
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Katayama, S., Saeki, H. Water solubilization of glycated carp and scallop myosin rods, and their soluble state under physiological conditions. Fish Sci 73, 446–452 (2007). https://doi.org/10.1111/j.1444-2906.2007.01353.x
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DOI: https://doi.org/10.1111/j.1444-2906.2007.01353.x