Accelerative sliding of myosin-coated glass-beads under suspended condition from actin paracrystal.
The maximum sliding velocity of rabbit skeletal-muscle myosin is about 10 micron/sec under zero load and physiological conditions. We have found, however, that a large glass-bead (diameter, 65 micron) coated by rabbit skeletal myosin slides at 338 +/- 47 micron/sec under a condition suspended from an actin paracrystal surface. Also the sliding velocity increases exponentially as the size of myosin-coated glass-beads increases. We report here that the sliding velocity of myosin can be controlled by the adhesion force and the external normal force acting between actin and myosin.
Suda
H
H
Department of Biological Science and Technology, Tokai University, 317 Nishino, Numazu, Shizuoka, 410-03, Japan.
Ishikawa
A
A
D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D003460:Crystallization; D005898:Glass; D018482:Muscle, Skeletal / Q000737:chemistry; D009218:Myosins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011817:Rabbits
D000199:Actins; D009218:Myosins