Effect of postmortem storage on the Z-line region of titin in bovine muscle.

Myofibrils were prepared from bovine muscles (cutaneous trunci, rectus abdominis, psoas major, and masseter) and compared between different aging periods at 4 degrees C (0, 1, 2, 4, 8, and 16 d). Myofibrils were stained with an antibody directed against a 56-kDa fragment (FE-RE) of titin located in the Z-line region. Unaged myofibrils from all four muscles showed a single stained band at the Z-line with similar intensities. Postmortem time did not significantly affect the total amount of fluorescence in the sarcomere, suggesting the titin FE-RE epitope was not degraded nor were titin fragments containing this epitope released during storage. However, the fluorescence patterns were altered. The relative fluorescence intensity at the Z-line decreased but that in the I-band increased gradually, showing the translocation of some titin FE-RE epitopes during the aging period. This suggested that a cleavage occurred in a region of titin very close to the Z-line during postmortem storage. Usually the position of maximum fluorescence remained at the Z-line, although about 1/3 of the myofibrils from rectus abdominis showed a two-band pattern around the Z-line after 16 d of aging. The titin changes observed may be related to the increased fragility of the myofibril and the improvement of meat tenderness during postmortem storage.