Sugi H
School of Medicine,
Tokyo
Japan
Review Article
Evidence for the Regulation of Actin-myosin Binding Strength by Lever
Arm and Subfragment-2 Regions of Myosin Molecule in Contracting
Skinned Muscle Fibers as Revealed by the Effect of Antibodies
Author(s): Sugi H and Chaen SSugi H and Chaen S
It is generally believed that myosin heads (M) extending from myosin filaments form weak binding with actin filament (A) in the form of A-M-ADP-Pi, and strong binding with A in the form of A-M-ADP and A-M. During muscle contraction, M first attaches weakly to A in the form of M-ADP-Pi, and then release Pi to attach strongly with A in the form of A-MADP to exert power stroke producing myofilament sliding. The weak to strong binding transition between M and A is therefore essential for producing muscle contraction. After power stroke, associated with release of ADP, M detaches from A on binding with next ATP to form M-ADP-Pi. Thus, M repeats attachment-detachment cycle with A, coupled with ATP hydrolysis. Using antibodies to myosin lever arm domain (anti-LD antibody) and to myosin subfragment-2 region (anti-S-2 antibody), we have found that, if these antibodies attach to LD or S-2 regio.. View More»
DOI:
10.4172/2157-7439.1000415