The Journal of Cell Biology, Vol 82, 57-65, Copyright © 1979 by The Rockefeller University Press

ARTICLES

N-ethylmaleimide-modified heavy meromyosin. A probe for actomyosin interactions

RL Meeusen and WZ Cande

Treatment of rabbit skeletal muscle heavy meromyosin (HMM) with the sulfhydryl reagent N-ethylmaleimide (NEM) produces a species of HMM which remains tightly bound to actin in the presence of MgATP. NEM-HMM forms characteristic "arrowhead" complexes with actin which persist despite rinses with MgATP. NEM-HMM inhibits the actin activation of native HMM-ATPase activity, the superprecipitation of actomyosin, the contraction of glycerinated muscle myofibrils, and the contraction of cytoplasmic strands of the soil amoeba Chaos carolinensis. However, NEM- HMM does not interfere with in vitro microtubule polymerization or beating of demembranated cilia.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

• Gebhardt, J. C. M., Clemen, A. E.-M., Jaud, J., Rief, M. (2006). From the Cover: Myosin-V is a mechanical ratchet. Proc. Natl. Acad. Sci. USA 103: 8680-8685 [Abstract] [Full Text]  
• Yamashita, H., Sugiura, S., Fujita, H., Yasuda, S.-i., Nagai, R., Saeki, Y., Sunagawa, K., Sugi, H. (2003). Myosin light chain isoforms modify force-generating ability of cardiac myosin by changing the kinetics of actin-myosin interaction. Cardiovasc Res 60: 580-588 [Abstract] [Full Text]  
• Mandato, C. A., Bement, W. M. (2001). Contraction and polymerization cooperate to assemble and close actomyosin rings around Xenopus oocyte wounds. JCB 154: 785-798 [Abstract] [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents