Thick filaments of fish myosin and its actin-activated Mg-ATPase activity.
1. Tilapia (Tilapia nilotica) myosin forms short, mini-filaments, and are easily disassembled upon addition of ATP showing no saturated activation in its actin-activated Mg-ATPase activity. 2. The presence of 5-10 mM MgCl2 allows tilapia myosin to form native thick-filaments and are resistant to ATP. 3. The rod portion of Tilapia myosin molecule is responsible for its characteristic filament forming ability. 4. The similar filament forming ability as Tilapia myosin was suggested for other fish myosins.
Matsuura
M
M
Department of Food Science, Faculty of Fisheries, Hokkaido University, Japan.
Konno
K
K
Arai
K
K
D000199:Actins / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism*; D005399:Fishes / Q000378:metabolism*; D008274:Magnesium / Q000494:pharmacology; D015636:Magnesium Chloride; D008854:Microscopy, Electron; D009132:Muscles / Q000378:metabolism; D009218:Myosins / Q000378:metabolism* / Q000648:ultrastructure; D011817:Rabbits
D000199:Actins; D015636:Magnesium Chloride; D000255:Adenosine Triphosphate; D017301:Ca(2+) Mg(2+)-ATPase; D009218:Myosins; D008274:Magnesium