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Abstract

The original calpain structure involved three molecules: two Ca2 + -dependent proteases, mu-calpain and m-calpain, and a third peptide. Calpastatin is an endogenous protein macromolecule that has a significant effect on calpain. In addition, calpain activity is believed to be affected by free calcium concentration due to the presence of calpain inhibitor substances. μ-related degreed m-calpain is a heterodimer conferred by the indivisible 28-kDa fractional unit of currency and an 80-kDa subunit that shares 55-65% sequence similarity in both proteases. In human order, there are fourteen calpain genes. The most studied calpain, known as calpain, is ubiquitous. Calpains play an important role in the characterization of macromolecules, leading to improved meat quality after slaughter. Although macromolecular deprivation in muscle atrophy is improved, and muscle growth rate is limited. This review summarizes the standard features of some of the calpain frameworks as well as the importance of the animal science calpain framework
Keywords: Calpain; Calpain inhibitor; Meat tenderization; Skeletal muscle growth
http://dx.doi.org/10.19045/bspab.2018.70075