The Journal of General Physiology
VISIT JCB ONLINE!
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text (PDF, 763K)
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JGP
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lehman, W.
Right arrow Articles by Szent-Györgyi, A. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lehman, W.
Right arrow Articles by Szent-Györgyi, A. G.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
The Journal of General Physiology, Vol 59, 375-387, Copyright © 1972 by The Rockefeller University Press

ARTICLE

Activation of the Adenosine Triphosphatase of Limulus polyphemus Actomyosin by Tropomyosin

William Lehman 1 and Andrew G. Szent-Györgyi 1

1 From the Department of Biology, Brandeis University, Waltham, Massachusetts 02154

Purified actin does not stimulate the adenosine triphosphatase (ATPase) activity of Limulus myosin greatly. The ATPase activity of such reconstituted preparations is only about one-fourth the ATPase of myofibrils or of natural actomyosin. Actin preparations containing tropomyosin, however, activate Limulus myosin fully. Both the tropomyosin and the actin preparations appear to be pure when tested by different techniques. Tropomyosin combines with actin but not with myosin and full activation is reached at a tropomyosin-to-actin ratio likely to be present in muscle. Tropomyosin and actin of several different animals stimulate the ATPase of Limulus myosin. Tropomyosin, however, is not required for the ATPases of scallop and rabbit myosin which are fully activated by pure actin alone. Evidence is presented that Limulus myosin, in the presence of ATP at low ionic strength, has a higher affinity for actin modified by tropomyosin than for pure actin.

Submitted on September 7, 1971


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Cold Spring Harb Symp Quant BiolHome page
R. D. Bremel, J. M. Murray, and A. Weber
Manifestations of Cooperative Behavior in the Regulated Actin Filament during Actin-Activated ATP Hydrolysis in the Presence of Calcium
Cold Spring Harb Symp Quant Biol, January 1, 1973; 37(0): 267 - 275.
[Abstract] [PDF]


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