SUMMARY The solubility characteristics and starch gel electrophoretic properties of intracellular bovine muscle proteins from the longissimus dorsi and semitendinosus muscles were investigated during a 336‐hr post‐mortem aging period. The relationship of solubility and electrophoretic behavior to post‐mortem tenderization was also investigated. In the semitendinosus muscle, the solubility of sarcoplasmic protein was highest at slaughter and decreased as post‐mortem aging proceeded, but no change was observed in the longissimus dorsi muscle. Fibrillar protein was least ex‐tractable at 24 hr post‐mortem, but its solubility was significantly higher at 168 and 336 hr than at 24 hr post‐mortem in both muscles studied. The amount of extractable fibrillar nitrogen was negatively related to Warner‐Bratzler shear values as post‐mortem aging proceeded. The increase in amount of soluble fibrillar nitrogen during the post‐mortem aging periods of 24‐168, 24‐336, and 168‐336 hr was positively related to the decrease in shear value for the respective periods. Fifteen zones were definable in the starch gel electrophoretic patterns of the sarcoplasmic proteins. At the pH used in this experiment, most of the zones were anionic. These anionic zones exhibited more discrete boundaries in the latter stages of aging, and certain new zones appeared or increased in intensity as aging progressed.
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Aberle et al. (1966) studied this question.
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