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Static and Dynamic X-Ray Diffraction Recordings from Living Mammalian and Amphibian Skeletal Muscles

Hiroyuki Iwamoto ^*, Jun'ichi Wakayama ^*, Tetsuro Fujisawa  and Naoto Yagi ^*

^* Life and Environment Division, SPring-8, Japan Synchrotron Radiation Research Institute, Hyogo 679-5198, Japan; and Structural Biochemistry Laboratory, RIKEN Harima Institute, SPring-8, Hyogo 679-5148, Japan

Correspondence: Address reprint requests to Dr. Hiroyuki Iwamoto, Life and Environment Division, SPring-8, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Mikazuki-cho Sayo-gun, Hyogo 679-5198, Japan. Tel.: +81-791-58-2507; Fax: +81-791-58-0830; E-mail: iwamoto{at}spring8.or.jp.

Static and time-resolved two-dimensional x-ray diffraction patterns, recorded from the living mouse diaphragm muscle, were compared with those from living frog sartorius muscle. The resting pattern of mouse muscle was similar to that of frog muscle, and consisted of actin- and myosin-based reflections with spacings basically identical to those of frog. As a notable exception, the sampling pattern of the myosin layer lines (MLL's) indicated that the mouse myofilaments were not organized into a superlattice as in frog. The intensity changes of reflections upon activation were also similar. The MLL's of both muscles were markedly weakened. Stereospecific (rigorlike) actomyosin species were not significantly populated in either muscle, as was evidenced by the 6th actin layer line (ALL), which was substantially enhanced but without a shift in its peak position or a concomitant rise of lower order ALL's. On close examination of the mouse pattern, however, a few lower order ALL's were found to rise, slightly but definitely, at the position expected for stereospecific binding. Their quick rise after the onset of stimulation indicates that this stereospecific complex is generated in the process of normal contraction. However, their rise is still too small to account for the marked enhancement of the 6th ALL, which is better explained by a myosin-induced structural change of actin. Since the forces of the two muscles are comparable regardless of the amount of stereospecific complex, it would be natural to consider that most of the force of skeletal muscle is supported by nonstereospecific actomyosin species.

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