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Thermal Gelation Characteristics of Myosin Subfragments
Author(s) -
SANO TAKESHI,
NOGUCHI SATOSHI F.,
MATSUMOTO JUICHIRO J.,
TSUCHIYA TAKAHIDE
Publication year - 1990
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.1365-2621.1990.tb06015.x
Subject(s) - heavy meromyosin , myosin , chemistry , viscoelasticity , meromyosin , biophysics , molecule , myosin head , myosin light chain kinase , biochemistry , materials science , organic chemistry , biology , composite material
To elucidate the roles of the head and the tail portions of the molecule in the thermal gelation of myosin, the gelation characteristics of heavy meromyosin (HMM) and of light meromyosin (LMM) were investigated. The aggregation process of HMM corresponded to that of myosin alone in the temperature range above 50°C. Both the dynamic viscoelastic behavior and the aggregation process of LMM agreed fairly well with those of myosin alone in the temperature range up to 45 °C. Therefore, the first development of gel elasticity of myosin was attributable mainly to the tail portion of the molecule and the second was to its head portion.

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