Distance of myofilament sliding per ATP molecule in skeletal muscle fibers studied using laser flash photolysis of caged ATP.
We studied the distance of myofilament sliding per hydrolysis of one ATP molecule by recording shortening of single glycerinated muscle fibers induced by laser flash photolysis of caged ATP, diffusion of photochemically released ATP out of the fiber being prevented by surrounding the fiber with silicone oil. With 75 microM ATP released (one half of the total myosin head concentration within the fiber), the fiber showed the minimum shortening (10 +/- 2 nm/half sarcomere, n = 10) taking place uniformly in each sarcomere in the fiber. Comparison of the initial flash-induced shortening velocity with the force-velocity relation of maximally Ca(2+)-activated fibers indicated that the above minimum fiber shortening took place under an internal load nearly equal to Po. These results may be taken to indicate that, under a nearly isometric condition, the distance of myofilament sliding per hydrolysis of one ATP molecule is of the order of 10 nm.
Yamada
T
T
Department of Physiology, School of Medicine, Teikyo University, Tokyo, Japan.
Abe
O
O
Kobayashi
T
T
Sugi
H
H
D008841:Actin Cytoskeleton / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000737:chemistry / Q000502:physiology*; D000818:Animals; D007537:Isometric Contraction / Q000502:physiology; D007834:Lasers; D009132:Muscles / Q000502:physiology* / Q000648:ultrastructure; D015879:Myosin Subfragments / Q000378:metabolism / Q000502:physiology; D010782:Photolysis; D016658:Psoas Muscles / Q000502:physiology; D011817:Rabbits; D012518:Sarcomeres / Q000502:physiology / Q000648:ultrastructure
D015879:Myosin Subfragments; D000255:Adenosine Triphosphate