X-RAY-DIFFRACTION STUDY ON MAMMALIAN VISCERAL SMOOTH MUSCLES IN RESTING AND ACTIVATED STATES

Structural changes of guinea pig taenia coli and rat anococcygeus muscle during contraction were studied by X-ray diffraction. The diffraction pattern of the taenia coli showed the 14.4-nm myosin reflection, the 5.9-nm actin layer-line and a diffuse equatorial peak at 1/11.4 nm(-1). On application of carbachol, the muscle contracted and the intensity of the 14.4-nm reflection showed a concentration-dependent decrease: the maximum decrease was 24% at 2x10(-5) M. Such an intensity decrease was not observed in K-contracture (154 mM). The intensity of the 5.9-nm actin layer-line did not change appreciably on activation. The equatorial peak became broader during contraction. The 14.4-nm myosin reflection of the anococcygeus muscle was weak. Its intensity increased by 106% during contraction induced by 2x10(-5) M phenylephrine and by 75% during K-contracture. These results suggest that the number of myosin filaments may increase during contraction of rat anococcygeus muscle but not guinea pig taenia coli.