Heat-induced structural changes and aggregation of walleye pollack myosin in the light meromyosin region

Fisheries Science

Volumn 68, Issue 5, 2002, Pages 1145-1150

  Higuchi, Tomoyuki ^a   Ojima, Takao ^a   Nishita, Kiyoyoshi ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

Author keywords

helix; Aggregation; Coprecipitation; Hydrophobicity; Light meromyosin; Myosin; Unfolding; Walleye pollack

Indexed keywords

POLLACHIUS POLLACHIUS; STIZOSTEDION VITREUM;

EID: 0036776140     PISSN: 09199268     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1444-2906.2002.00545.x     Document Type: Article

References (20)

1. Fukazawa T, Hashimoto Y, Yasui T. The relationship between the components of myofibrillar protein and the effect of various phosphates that influence the binding quality of sausage. J. Food Sci. 1961; 26: 550-555.
2. Iwata K, Kanna K, Okada M. Kamaboko formation of mackerel and red seabream myosins. Nippon Suisan Gakkaishi 1977; 43: 237.
3. Akahane T, Chihara S, Yoshida Y, Tsuchiya T, Noguchi S, Ookami H, Matsumoto JJ. Roles of constituent proteins in gel properties of cooked meat gels. Nippon Suisan Gakkaishi 1984; 50: 1029-1033.
4. Numakura T, Seki N, Kimura I, Toyoda K, Fujita T, Takama K, Arai K. Cross-linking reaction of myosin in the fish paste during setting (SUWARI). Nippon Suisan Gakkaishi 1985; 51: 1559-1565.
5. Samejima K, Ishioroshi M, Yasui T. Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin. J. Food Sci. 1981; 46: 1412-1418.
6. Ishioroshi M, Samejima K, Yasui T. Further studies on the roles of the head and tail regions of the myosin molecule in heat-induced gelation. J. Food Sci. 1981; 47: 114-120.
7. Sano T, Noguchi F, Matsumoto JJ, Tsuchiya T. Thermal gelation characteristics of myosin subfragments. J. Food Sci. 1990; 55: 55-58, 70.
8. Morita J, Yasui T. Involvement of hydrophobic residues in heat-induced gelation of myosin tail subfragments from rabbit skeletal myosin. Agric. Biol. Chem. 1991; 55: 597-599.
9. Chan JK, Gill TA, Paulson AT. Thermal aggregation of myosin subfragments from cod and herring. J. Food Sci. 1993; 58: 1057-1061, 1069.
10. Ogawa M, Kanamaru J, Miyashita H, Tamiya T, Tsuchiya T. Alpha-helical structure of fish actomyosin: Changes during setting. J. Food Sci. 1995; 60: 297-299.
11. Ojima T, Yoshikawa S, Nishita K. Isolation and characterization of myosin from walleye pollack surimi. Fish. Sci. 1997; 63: 811-815.
12. Ojima T, Higuchi T, Nishita K. Reversibility of unfolding of walleye pollack light meromyosin by heat-treatment. Fish. Sci. 1999; 65: 459-465.
13. Ojima T, Kawashima N, Inoue A, Amauchi A, Togashi M, Watabe S, Nishita K. Determination of primary structure of heavy meromyosin region of walleye pollack myosin heavy chain by cDNA cloning. Fish. Sci. 1998; 64: 812-819.
14. Togashi M, Kakinuma M, Hirayama Y, Fukushima H, Watabe S, Ojima T, Nishita K. cDNA cloning of myosin rod and the complete primary structure of myosin heavy chain of walleye pollack fast skeletal muscle. Fish. Sci. 2000; 66: 349-357.
15. Wu CS, Yang JT. Reexamination of the conformation of muscle proteins by optical activity. Biochemistry 1976; 15: 3007-3014.
16. Niwa E, Sato K, Suzuki R, Nakayama T. Fluorometric study of setting properties of fish flesh sol. Nippon Suisan Gakkaishi 1981; 47: 817-821.
17. Porzio MA, Pearson AM. Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochim. Biophys. Acta 1977; 490: 27-34.
18. Gornall AG, Bardawill CJ, David MM. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 1949; 177: 751-765.
19. Pastra-Landis SC, Lowey S. Myosin subunit interactions. Properties of the 19,000-dalton light chain-deficient myosin. J. Biol. Chem. 1986; 261: 14 811-14 816.
20. Sharp A, Offer G. The mechanism of formation of gels from myosin molecules. J. Sci. Food Agric. 1992; 58: 63-73.