Abstract
Similarity in the mechanism of contraction in smooth and skeletal muscle is based on the presence of contractile proteins, similar or identical in structure, properties and biological activity, in both types of muscle. Troponin, which together with tropomyosin confers calcium sensitivity to actomyosin, is shown to be present in bovine uterine smooth muscle. Uterine troponin was purified by isoelectric precipitation and ammonium sulfate fractionation. The uterine troponin preparations were shown to be free of tropomyosin in acrylamide gel electrophoresis. Electrophoresis in sodium dodecyl sulfate showed a minimum of six components. The intrinsic viscosity of uterine troponin was greatly increased upon addition of uterine tropomyosin indicating complex formation of the two proteins. The biological activity of uterine troponin was similar to that of skeletal troponin. The uterine troponin-tropomyosin complex inhibited uterine and skeletal actomyosin ATPase in the presence of EGTA.
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