Weakening of the Z-disks of skeletal muscle myofibrils contributes to the tenderization of meat during post-mortem aging. To elucidate the weakening mechanism, we compared Z-disks weakened by post-mortem aging of chicken breast muscle with those of myofibrils treated with a solution containing 0.1 mM CaCl2 and 1 μM calpastatin domain I. In both cases, the Z-disks were weakened with a corresponding liberation of their constituent phospholipids (PLs). The liberation of PLs specific to 0.1 mM calcium ions was minimal at pH 6.5 and maximal at 35°C together with the Z-disk weakening. Binding of calcium ions to PLs in the Z-disks was determined by 45Ca-autoradiography. Acidic PLs were strongly radioactive and neutral PLs were appreciably radioactive. It is very probable that acidic PLs would bind electrostatically to α-actinin under physiological conditions, and that this interaction would be broken by the binding of calcium ions at 0.1 mM to PLs, resulting in the partial liberation of PLs from Z-disks. We conclude, therefore, that the liberation of PLs by the binding of 0.1 mM calcium ions was the main cause for Z-disk weakening during the post-mortem aging of chicken. © 1998, Taylor & Francis Group, LLC. All rights reserved.
CITATION STYLE
Shimada, K. I., Ahn, D. H., & Takahashi, K. (1998). Liberation of phospholipids from Z-disks of chicken skeletal muscle myofibrils by 0.1 mM Calcium ions: Weakening mechanism for Z-disks during post-mortem aging of meat. Bioscience, Biotechnology and Biochemistry, 62(5), 919–926. https://doi.org/10.1271/bbb.62.919
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