Study of reciprocal effects of cardiac myosin and tropomyosin isoforms on actin-myosin interaction with in vitro motility assay.
Interaction of myosin with actin in striated muscle is controlled by Ca(2+) via thin filament associated proteins: troponin and tropomyosin. In cardiac muscle there is a whole pattern of myosin and tropomyosin isoforms. The aim of the current work is to study regulatory effect of tropomyosin on sliding velocity of actin filaments in the in vitro motility assay over cardiac isomyosins. It was found that tropomyosins of different content of α- and β-chains being added to actin filament effects the sliding velocity of filaments in different ways. On the other hand the velocity of filaments with the same tropomyosins depends on both heavy and light chains isoforms of cardiac myosin.
Institute of Immunology and Physiology, Russian Academy of Sciences, Yekaterinburg 620041, Russia. d.shchepkin@iip.uran.ru
D V
DV
Shchepkin
G V
GV
Kopylova
L V
LV
Nikitina
D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001681:Biological Assay; D024722:Cardiac Myosins / Q000737:chemistry / Q000378:metabolism*; D002417:Cattle; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism; D011817:Rabbits; D014335:Tropomyosin / Q000737:chemistry / Q000378:metabolism*
D000199:Actins; D020033:Protein Isoforms; D014335:Tropomyosin; D024722:Cardiac Myosins