The effects of ionic strength on myofibrils and myosin from rabbit fast‐twitch Psoas major (PM) and slow‐twitch Semimembranosus proprius (SMp) muscles before and after heating were studied by electron microscopy and thermal scanning rheometry. The direct suspension of proteins in low ionic strength (0.2M KCl; pH 6.0) led to very weak gels, whereas a gradual lowering of the ionic strength (by dialysis against 0.2M KCl; pH 6.0) of 0.6M KCl protein solutions induced strand‐type networks at low temperature and strong heat‐induced gels. As shown by transmission and scanning electron micrographs, in low ionic strength, SMp myosins formed shorter filaments before heating and thinner and shorter structures in heat‐induced gels, as well as a lower gel porosity than PM myosins.
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Boyer et al. (1996) studied this question.
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