An X-ray diffraction study on a single frog skinned muscle fiber in the presence of vanadate.
Using a technique to obtain a detailed X-ray diffraction pattern from a single frog skinned muscle fiber with synchrotron radiation and an imaging plate, we studied the arrangement of myosin heads to which ADP and vanadate are bound. The presence of 1 mM vanadate during contraction caused trapping of ADP and vanadate on the myosin head. Both in the presence and absence of Ca2+, the intensities of the equatorial reflections indicated that most of the heads with ADP and vanadate were located close to the backbone of the thick filament. The presence of the first myosin layer-line at 43 nm-1 also suggested that the heads formed a helix around the shaft of the thick filament. Weak intensity of actin layer-lines suggested that the myosin heads were detached from the thin filament. The results suggest that the myosin-ADP-vanadate complex has a weak affinity toward actin regardless of the state of the regulatory system on the thin filament.
Takemori
S
S
Department of Physiology, Jikei University School of Medicine, Tokyo.
Yamaguchi
M
M
Yagi
N
N
D000244:Adenosine Diphosphate / Q000737:chemistry*; D000818:Animals; D018485:Muscle Fibers, Skeletal / Q000187:drug effects* / Q000648:ultrastructure; D018482:Muscle, Skeletal / Q000187:drug effects* / Q000648:ultrastructure; D009218:Myosins / Q000737:chemistry*; D011892:Rana catesbeiana; D014638:Vanadates / Q000737:chemistry / Q000494:pharmacology*; D014961:X-Ray Diffraction
D014638:Vanadates; D000244:Adenosine Diphosphate; D009218:Myosins