Thermal Aggregation of Myosin Subfragments from Cod and Herring

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<jats:title>ABSTRACT</jats:title><jats:p>Turbidity of fish myosin subfragment solutions increased with temperature, except cod heavy meromyosin turbidity leveled above 45°C. Extent of aggregation and number of cross‐linking sites for cod heavy and light meromyosins were significantly higher than for herring (p<0.05), but only at temperatures above 35°C and 45°C, respectively. Thermal aggregation ability increased linearly with increased surface hydrophobicity (S<jats:sub>o</jats:sub>) for the myosin subfragments, except cod heavy meromyosin where the increase in S<jats:sub>o</jats:sub> between 45–55°C did not correspond to an increase in cross‐linking ability. The lessened aggregation ability of herring myosins may be due to the low cross‐linking of the HMM (S‐2) region.</jats:p>

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