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study, caspases were found to be most active mortem proteolysis. A negative relationship
early postmortem (<4 hr), and caspase activ- between peak caspase 3/7 activity at 8 hours
ity diminished with postmortem time. It was postmortem and calpastatin activity at 0 and
also observed that caspase activity (caspase 2 days postmortem has been observed in the
3/7 and caspase 9) and the abundance of muscles of normal lambs but not in callipyge
alpha II spectrin degradation products were lambs (Kemp et al. 2009). Thus, while there
negatively correlated to Warner-Bratzler is no direct evidence that caspases contribute
shear force measurements. This led to the significantly to postmortem tenderization,
conclusion that the changes in caspase data suggest that they may play an indirect
activity and caspase-mediated cleavage of role by degrading calpastatin. More data is