The Journal of General Physiology
Sign up for e-mail content alerts
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article
Right arrow Full Text (PDF, 906K)
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 Kawai, M.
Right arrow Articles by Brandt, P. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kawai, M.
Right arrow Articles by Brandt, P. W.
Right arrowPubmed/NCBI databases
*Compound via MeSH
*Substance via MeSH
Hazardous Substances DB
*CALCIUM COMPOUNDS
*CALCIUM, ELEMENTAL
*ETHYLENEDIAMINE TETRAACETIC ACID
*MAGNESIUM COMPOUNDS
*MAGNESIUM, ELEMENTAL
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

The Journal of General Physiology, Vol 68, 267-280, Copyright © 1976 by The Rockefeller University Press


ARTICLES

Two rigor states in skinned crayfish single muscle fibers

M Kawai and PW Brandt

We studied the tension and stiffness of crayfish skinned single muscle fibers during and after the induction of rigor by removal of MgATP (substrate). We found that the rigor state is not unique but depends on the condition of the muscle before rigor. Fibers induced into rigor with a minimum of activation (low rigor) develop a small tension and moderate stiffness, while those entering rigor during maximum activation (high rigor) maintain near peak tension (80%) and develop a high stiffness. These rigor states are insensitive to Ca addition or deletion but they are partially interconvertible by length change. Stiffness changes when the rigor muscle length is varied, a condition in which the number of attached cross-rigor muscle length is varied, a condition in which the number of attached cross-bridges cannot change, and high-rigor muscle becomes less stiff than low-rigor muscle when the former is brought to the same tension by length release. The sensitivity of low, high, or length-released high-rigor muscles to trace substrate concentration (less than muM) differs, and rigor at lower strain is more suscepitible to substrate.
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 Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
J. Physiol.Home page
X. Lu, M. K Bryant, K. E Bryan, P. A Rubenstein, and M. Kawai
Role of the N-terminal negative charges of actin in force generation and cross-bridge kinetics in reconstituted bovine cardiac muscle fibres
J. Physiol., April 1, 2005; 564(1): 65 - 82.
[Abstract] [Full Text] [PDF]


Home page
J. Physiol.Home page
H. Fujita, D. Sasaki, K. Fukuda, and S. Ishiwata
Myosin light chain 2 modulates MgADP-induced contraction in rabbit skeletal and bovine cardiac skinned muscle
J. Physiol., July 1, 2002; 542(1): 221 - 229.
[Abstract] [Full Text] [PDF]



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