Interaction of Protein-Bound Polysaccharide (PS-K) with Rabbit Skeletal Muscle Actomyosin

概要

論文の詳細を見る
The interaction of protein-bound polysaccharide (PS-K) with actomyosin from rabbit skeletal muscle was investigated by measuring the changes in adenosine triphosphatase (ATPase) activity, turbidity, and viscosity. At low ionic strengths, PS-K reduced the actin-activated Mg^<2+>-ATPase activity of myosin to 20% of the original level, whereas it slightly enhanced the myosin ATPase activity without actin. The inhibition of actin-activated ATPase activity was not reversed by increasing actin concentration and, further, the apparent affinity of myosin for actin was not altered by the addition of PS-K. The extent of inhibition depended on the sequence of addition of myosin, actin, and PS-K, i. e., when PS-K was preincubated first with myosin before adding actin, the most marked inhibition was observed. The changes of actomyosin turbidity induced by PS-K were similar to those of ATPase inhibition. PS-K did not affect the polymerization and depolymerization of actin. Therefore, the inhibitory effects seem to be caused by PS-K bound to myosin filaments.
公益社団法人日本薬学会の論文
1985-08-25