A myosin/actomyosin mixture (MAM), actomyosin and myosin were isolated from post‐rigor turkey. Rheological properties of MAM gels were determined by uniaxial compression. Breast MAM formed gels which were stable at lower protein concentrations (10 and 15 mg/mL) than thigh MAM (20 and 25 mg/mL). Differential scanning calorimetry (DSC) and a fluorescent hydrophobic probe, 8‐anilino‐l‐napthalene sulfonate (ANS), were used to study thermal transitions. One DSC peak was observed in breast and thigh MAM. ANS thermograms showed that thigh actomyosin had a greater transition temperature (Tr) (51.8°C) than breast actomyosin (49.7°C). The ANS Tr was 48°C for both myosins. The difference in gelation appeared to be associated with protein‐protein interactions.
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DUDZIAK et al. (1988) studied this question.
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