Further Studies on the Roles of the Head and Tall Regions of the Myosin Molecule in Heat‐induced Gelation

MAKOTO ISHIOROSHI, KUNIHIKO SAMEJIMA, TSUTOMU YASUI

doi:10.1111/j.1365-2621.1982.tb11040.x

Further Studies on the Roles of the Head and Tall Regions of the Myosin Molecule in Heat‐induced Gelation

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<jats:title>ABSTRACT</jats:title><jats:p>Heat induced gelation properties of the two proteolytic fragments of myosin, heavy (HMM) and light meromyosin (LMM), were studied by rigidity measurement in a band type viscometer and by a direct examination using a scanning electron microscope. A heat induced network forming ability for both LMM and HMM was found in 0.6M KCl at a pH 6.0. LMM produced gels corresponding to a reversible helix‐coil transition at temperatures ranging from 40–70°C, with little evidence of aggregation as assessed from a turbidity change of the system. Contrary, HMM associated irreversibly producing a gel with increased rigidity at pH 5.0 and a salt concentration of 0.1 M. Oxidation of SH‐groups appeared to be involved only in HMM and not in LMM gelation process.</jats:p>