Abstract
The in vitro assembly of myosin purified from calf aorta muscle has been studied by electron microscopy. Two types of filament are formed: short bipolar filament similar to those formed from skeletal muscle myosin, and longer "side-polar" filaments having cross bridges with a single polarity along the entire length of one side and the opposite polarity along the other side. Unlike the case with skeletal myosin filaments, antiparallel interactions between myosin molecules occur along the whole length of side-polar filaments. The side-polar structure may be related to the in vivo form of myosin in vertebrate smooth muscle.
Dates
Type | When |
---|---|
Created | 21 years, 3 months ago (May 14, 2004, 7:04 p.m.) |
Deposited | 2 years, 1 month ago (July 24, 2023, 4:05 a.m.) |
Indexed | 1 month, 1 week ago (July 22, 2025, 7:21 a.m.) |
Issued | 47 years, 9 months ago (Dec. 1, 1977) |
Published | 47 years, 9 months ago (Dec. 1, 1977) |
Published Online | 47 years, 9 months ago (Dec. 1, 1977) |
Published Print | 47 years, 9 months ago (Dec. 1, 1977) |
@article{Craig_1977, title={Assembly of smooth muscle myosin into side-polar filaments.}, volume={75}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.75.3.990}, DOI={10.1083/jcb.75.3.990}, number={3}, journal={The Journal of cell biology}, publisher={Rockefeller University Press}, author={Craig, R and Megerman, J}, year={1977}, month=dec, pages={990–996} }