Species-specific thermal denaturation pattern of fish myosin when heated as myofibrils as studied by myosin subfragment-1 and rod denaturation rates |
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| Authors: | Masayuki?Takahashi Takeshi?Yamamoto Sanae?Kato Email author" target="_blank">Kunihiko?KonnoEmail author |
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| Institution: | (1) Laboratory of Marine Food Sciences, Graduate School of Fisheries Science, Hokkaido University, 041-8611 Hakodate, Hokkaido, Japan;(2) Present address: Department of Biochemistry, Asahikawa Medical College, 078-8510 Asahikawa, Japan |
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| Abstract: | Thermal denaturation of myofibrils from various species of fish was investigated by measuring ATPase inactivation, myosin
aggregation, myosin subfragment-1 (S-1) and rod denaturation rates as studied by chymotryptic digestion. Decrease in monomeric
myosin (myosin aggregation) was always faster than the ATPase inactivation for all myofibrils tested. The relative denaturation
rate of rod to that of S-1 differed from species to species. Preceded denaturation of rod was observed with some species,
and the opposite was true with other species. The denaturation pattern was explained by the different magnitude of S-1 stabilization
by F-actin in myofibrils at low salt medium. Myofibrils which receive a great stabilization by F-actin as studied by ATPase
inactivation showed the preceded rod denaturation pattern, and vice versa. S-1 portion, not F-actin, determined the different
stabilization of S-1 by F-actin in myofibrils. |
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| Keywords: | F-actin myofibril myosin species specificity thermal denaturation |
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