Liha töötlemine
released them from the sarcomere, the main to release proteins from the myofibrillar
candidate is the proteasome (Attaix et al. assembly in order to make large proteins
1998, 2001; Delbarre-Ladrat et al. 2006; available for degradation into amino acids by
Yamamoto et al. 2009; Geesink and Veiseth the MCP (Hasselgren 1999; Allen and Goll
2009). 2003). The MCP plays a major role in degrad-
The proteasome, or multicatalytic protein- ing sarcoplasmic proteins and myofibrillar
ase complex (MCP), is a multisubunit prote- fragments; however, there is insufficient evi-
ase complex with an apparent sedimentation dence that MCP breaks down the same pro-
coefficient of 20S. Two types of regulatory teins in postmortem muscle as in in vitro tests
complexes bind to both ends of the cylindri- (Huang et al. 2007). Proteasomes remained
cal 20S