Liha töötlemine
substrate accessibility. Lysosomes are inca- et al. 1990; Spencer et al. 1995; Sorimachi
pable of engulfing the myofibril structure and and Suzuki 2001; Huang and Wang 2001).
no myofibrillar fragments have been identi- The Ca2+ requirements, optimum pH and
Aging/Tenderization Mechanisms 89
temperature of activity, autolysis, and inhibi- Geesink et al. 2005). Although the mRNA
tors of calpains have been extensively levels for p94 are 10 times greater than μ-
reviewed (Allen and Goll 2003; Geesink and and m-calpain mRNA (Kinbara et al. 1998),
Veiseth 2009). Calpain 1, or μ-calpain, purification from muscle is difficult because
requires micromolar (10–50 μM) calcium it is highly unstable. The p94 has both a cys-
concentration for full activity
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