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DEGRADATION OF MYOFIBRILLAR PROTEIN COMPONENTS DURING POSTMORTEM AGING OF CHICKEN MUSCLE
Author(s) -
SAMEJIMA K.,
WOLFE F. H.
Publication year - 1976
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.1365-2621.1976.tb00595.x
Subject(s) - myofibril , actin , chemistry , biochemistry , fibril , electrophoresis , atpase , biophysics , anatomy , biology , enzyme
A 30,000 dalton protein is produced from chicken muscle fibrils as a result of postmortem aging. The myofibrils of fresh muscle homogenates incubated at a temperature of 40°C for 4 hr at pH 5.4 also develop this band. Purified myofibrils treated in this manner show no changes in electrophoretic pattern. Changes in ATPase activities of myofibrils as a function of pH are unrelated to the development of the 30,000 band. Electrophoretic patterns of natural F‐actin prepared from aged muscle also exhibit a 30,000 band, suggesting that this band may be associated with thin filaments.