Enhancement of the actin-activated ATPase activity of myosin from canine cardiac ventricle by purealin.
The effects of purealin isolated from the sea sponge, Psammaplysilla purea, on the enzymatic properties of myosin and natural actomyosin (a complex of myosin, actin, tropomyosin and troponin) from canine cardiac ventricle were studied. Purealin increased the ATPase activity of natural actomyosin and the actin-activated ATPase activity of myosin, and accelerated the superprecipitation of natural actomyosin. The Ca2+- and Mg2+-ATPase activities of myosin were inhibited by purealin, whereas the K+-EDTA-ATPase activity was increased. These results suggest that purealin binds to the myosin portion involved in actin-myosin interaction and increases the actin-activated ATPase activity of myosin.
D000199:Actins / Q000494:pharmacology*; D000205:Actomyosin / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D001969:Bromobenzenes / Q000378:metabolism / Q000494:pharmacology*; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D011232:Chemical Precipitation; D004285:Dogs; D004789:Enzyme Activation / Q000187:drug effects; D006352:Heart Ventricles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology*; D009218:Myosins / Q000378:metabolism*
D000199:Actins; D001969:Bromobenzenes; C050163:purealin; D000205:Actomyosin; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; C026049:EDTA-ATPase; D009218:Myosins; D000252:Calcium-Transporting ATPases