Relative Roles of the Head and Tail Portions of the Molecule in Heat-Induced Gelation of Myosin |
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| Authors: | KUNIHIKO SAMEJIMA MAKOTO ISHIOROSHI TSUTOMU YASUI |
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| Affiliation: | Author Samejima is with the Dept. of Dairy Science, The College of Dairying, Ebetsu City, Hakkaida, Japan, 069-01.;Authors Ishioroshi and Yasui are with the Dept. of Animal Science, Faculty of Agriculture of Hakkaido Univ., Sapparo, Hakkaido, Japan, 061. |
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| Abstract: | Myosin molecules are cleaved by chymotrypsin digestion into two fragments: subfragment 1, which originates from the globular heads of myosin, and the myosin rod, which originates from the helical tail of the myosin molecule. The heat-induced gelation of these subfragments was compared to that of intact myosin by measuring rigidity, turbidity, and other physico-chemical characteristics of each system. Two features of the heat-induced gelation of myosin, aggregation and three-dimensional network formation were found to be imparted by the subfragment 1 and the rod, respectively. The former involves disulfide exchange and the latter relates to conformational changes arising from a partially irreversible helix-coil transition during heating. Possible relationships are suggested between these physicochemical changes of the myosin head and tail regions upon heating and the heat-induced gelation of myosin. |
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