Contractile properties of actomyosin from human blood platelets.

摘要: Actomyosin was purified from human blood platelets and used to form threads via extrusion. A sensitive tensiometer employed measure isometric tension velocity of isotonic shortening the in presence MgATP. Using fully phosphorylated myosin, we obtained values for maximum (Po) contraction (V max) that were similar those reported composed skeletal muscle actomyosin. Po found be directly proportional level phosphorylation 20,000-dalton myosin light chain. We also studied effect on superprecipitation platelet Fully produced rapid clearing superprecipitation, while with a low bound phosphate underwent but did not superprecipitate. have concluded these results that: 1) interaction between actin produces motion is by 2) chain important controlling production force myosin.