Liha töötlemine
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). Chicken endogenous N-terminal (but not C-terminal)
muscle expresses a distinct μ/m-calpain, domain of p94 is localized in the Z-bands and
intermediate to μ- and m-calpains in Ca2+ also directly binds to sarcomeric α-actinin,
requirements for activation (Sorimachi et al. suggesting incorporation of proteolytic frag-
1990; Sorimachi and Suzuki 2001; Lee et al
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