2+]-binding domain is linked to the catalytic domain II, which may regulate the activity of CAPN by participating in critical electrostatic interactions and the binding of phospholipids (Hosfield et al.
Location and function: What's more, most of CAPNs are intracellular: 70% of CAPN1 is bound to myofibrils, a large portion of CAPN3 is situated in a sarcomere near the N- and M-line, whereas a majority of CAPN2 is located in the cytosol (Ilian et al.
It is reported that the CAPN system makes a contribution to postmortem proteolysis and meat tenderization in domestic animals (Table 1) (Koohmaraie, 1992; Huff-Lonergan and Lonergan, 2005).
CAST inhibits CAPN1 and CAPN2 via the interaction between regions A, C and CAPNs when calcium binds to CAPNs: 40 |amol/L and 250 to 500 [micro]mol/L, respectively (Hanna et al.
Recent crystallographic observations have identified the nature of the interaction between CAST and CAPN, as to the interaction between their unique aspects (regions A, B and C) as protein inhibitors and proteolytic enzymes (Hanna et al.
2+]-dependent proteolytic systems such as the CAPN system will be influenced and the key proteins involved in tenderization will not be degraded or modified.
According to the theory of enzymatic meat tenderization, the CAPN system can play a role in postmortem proteolysis and meat tenderness.
In spite of this, several researches have been conducted in domestic animals based on the theory of enzymatic meat tenderization especially the CAPN protease system.
A single nucleotide polymorphism in CAPN 1 associated with marbling score in Korean cattle.
In particular, the rate of pH decline is closely related to the extent of proteolysis of myofibrillar proteins by CAPNs, such as the production of PSE pork (Barbut et al.