DEGRADATION OF MYOFIBRILLAR PROTEIN COMPONENTS DURING POSTMORTEM AGING OF CHICKEN MUSCLE

摘要

ABSTRACTA 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 filamen