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minal region (Muroya et al. 2007). Some ulatory complex that mediates actin-myosin studies have shown labeling of two very interactions (Greaser and Gergely, 1971; closely spaced bands corresponding to intact Hitchcock, 1975; McKay et al. 1997; Lehman troponin-T. This is likely due to isoforms of et al. 2001), it is also conceivable that its troponin-T that are known to exist in skeletal postmortem degradation may lead to changes muscle (Briggs et al. 1990; Malhotra 1994; involving thick and thin filament interac- Muroya et al. 2007), including specifically tions. Regardless of whether or not troponin- bovine skeletal muscle (Muroya et al. 2007). -T aids in disruption of the thin filament in Both the appearance of the 30- and 28-kDa the I-band, alters thick and thin filament bands and the disappearance of the intact interactions, or simply reflects overall protein
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