Tatsumi R, Takahashi K
Department of Animal Science, Faculty of Agriculture, Hokkaido University.
J Biochem. 1992 Dec;112(6):775-9. doi: 10.1093/oxfordjournals.jbchem.a123974.
When chicken breast muscle myofibrils were treated with a solution containing 0.1 mM CaCl2 and 30 micrograms of leupeptin/ml, nebulin filaments were fragmented into 200-, 180-, 40-, 33-, and 23-kDa subfragments. All the subfragments except the 180-kDa one were released from the myofibrils. The fragmentation of nebulin filaments seems to be induced by the binding of large amounts of calcium ions. Similar changes took place in nebulin filaments in post-mortem skeletal muscle. It has been proposed that nebulin co-exists with thin (actin) filaments and participates in stabilizing their organization [Wang, K. & Wright, J. (1988) J. Cell Biol. 107, 2199-2212]. Thus, the above result suggests that Ca-induced fragmentation of nebulin filaments destabilizes the organization of thin filaments and is a key factor in meat tenderization during post-rigor aging.
当鸡胸肌肌原纤维用含有0.1 mM氯化钙和30微克亮抑酶肽/毫升的溶液处理时，伴肌动蛋白丝被裂解成200 kDa、180 kDa、40 kDa、33 kDa和23 kDa的亚片段。除180 kDa的亚片段外，所有亚片段均从肌原纤维中释放出来。伴肌动蛋白丝的裂解似乎是由大量钙离子的结合所诱导的。宰后骨骼肌中的伴肌动蛋白丝也发生了类似的变化。有人提出，伴肌动蛋白与细（肌动蛋白）丝共存，并参与稳定其结构[Wang, K. & Wright, J. (1988) J. Cell Biol. 107, 2199 - 2212]。因此，上述结果表明，钙离子诱导的伴肌动蛋白丝裂解会破坏细肌丝的结构，并且是宰后成熟过程中肉嫩化的关键因素。
