[Changes in mackerel (Scomber scombrus, L.) skeletal muscle tissue during prolonged low-temperature preservation].
Freezing slightly changes ultrastructure of myofibrillar proteins, but is accompanied with their decreased solubility. During frozen storage, progressive decrease in solubility of these proteins by the 4th month is probably depended on the fact that in sarcoplasm certain globular particle associates appear; they are products of the most easily hydrolized proteins in filaments, namely, Z-lines, I-discs, H-zone. The fact that some protein components of the sarcomere disappear simultaneously with decreasing solubility of the myofibrillar proteins demonstrates that these processes are closely connected with each other.
D000818:Animals; D005399:Fishes / Q000033:anatomy & histology*; D005615:Freezing; D009124:Muscle Proteins; D009132:Muscles / Q000648:ultrastructure*; D009210:Myofibrils / Q000648:ultrastructure; D011489:Protein Denaturation; D012995:Solubility; D013997:Time Factors; D014021:Tissue Preservation
D009124:Muscle Proteins
Izmeneniia skeletnoĭ myshechnoĭ tkani skumbrii (Scomber scombrus, L) v protsesse dlitel'noĭ konservatsii kholodom.