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Further Studies on the Roles of the Head and Tall Regions of the Myosin Molecule in Heat‐induced Gelation
Author(s) -
ISHIOROSHI MAKOTO,
SAMEJIMA KUNIHIKO,
YASUI TSUTOMU
Publication year - 1982
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1982.tb11040.x
Subject(s) - heavy meromyosin , chemistry , myosin , rigidity (electromagnetism) , viscometer , molecule , crystallography , biophysics , analytical chemistry (journal) , chromatography , materials science , biochemistry , organic chemistry , biology , viscosity , composite material
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.