Liha töötlemine
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. Calpain 2, teine protease domain and a calmodulin-like
m-calpain, is activated at 0.3–1.0 mM Ca2+, Ca+2 binding domain in the same polypeptide
while the Ca2+ requirement of p94/calpain 3 chain that binds to the N2A and M-line
is reported to be at submicromolar levels regions of titin (Ojima et al. 2007). The
(Branca et al. 1999; Ono et al. 2004)
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