title: [Complex biochemical and structural study of skeletal muscles in scoliosis].
abstract: Structural study of human scoliosis muscles showed significant dystrophic and degenerative changes: desintegration of fibrillar structure and striation; the Zencker necrosis; the replacement of muscular tissue by connective and adipose tissues. The electron microscopic observation revealed disordering of filamental array of the sarcomere (I- and A-discs), the broadening of Z-disc material, the appearance of N-stripes in I-band. At the same time deviations from the norm were observed in contractile proteins: actin and myosin. ATPase activity of myosin decreased by 25--30%; the flow of birefringence of myosin and especially of actin also decreased. Actin from the scoliosis muscles partially or completely lost the ability for polymerization in 0.1 M KC1.
mesh_terms: D000199:Actins / Q000032:analysis; D000251:Adenosine Triphosphatases / Q000032:analysis; D000293:Adolescent; D002648:Child; D006801:Humans; D008854:Microscopy, Electron; D009132:Muscles / Q000032:analysis / Q000473:pathology* / Q000648:ultrastructure; D009210:Myofibrils / Q000648:ultrastructure; D009218:Myosins / Q000032:analysis; D012600:Scoliosis / Q000378:metabolism / Q000473:pathology*
chemical_list: D000199:Actins; D000251:Adenosine Triphosphatases; D009218:Myosins
vernacular_title: Kompleksnoe biokhimicheskoe i struktornoe issledovanie skeletnykh myshts pri skolioze.