spacer gif spacer gif spacer gif spacer gif Propose a Workshop for 2011 spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Holt, S. M.
Right arrow Articles by Kinsey, S. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Holt, S. M.
Right arrow Articles by Kinsey, S. T.
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   Add to Twitter  
What's this?
The Journal of Experimental Biology 205, 1775-1785 (2002)
© 2002 The Company of Biologists Limited

Osmotic effects on arginine kinase function in living muscle of the blue crab Callinectes sapidus

Stewart M. Holt* and Stephen T. Kinsey{dagger}

Department of Biological Sciences, University of North Carolina at Wilmington, 601 South College Road, Wilmington, NC 28403-3297, USA
* Present address: Department of Biology, University of Vermont, Burlington, VT 05405, USA

{dagger} Author for correspondence (e-mail: kinseys{at}uncwil.edu )

Accepted 8 April 2002

Flux was examined through the reaction catalyzed by arginine kinase in intact blue crab (Callinectes sapidus) muscle during simulated changes in salinity. Isolated dark levator muscles from the swimming leg were superfused with a saline solution that had an osmolarity equivalent to that of the hemolymph under different salinity regimes. Animals were acclimated for 7 days to a salinity of 5, 17 or 35{per thousand}, which corresponds to a hemolymph osmolarity of 640, 720 or 960 mosmoll-1, respectively. Experiments were conducted under control conditions, in which the osmolarity of the superfusion medium matched that of the acclimated hemolymph, as well as under hypo- and hyperosmotic conditions. These latter treatments were meant to simulate a rapid change in environmental salinity. Pseudo-first-order unidirectional rate constants and flux rates were measured for arginine kinase in the forward and reverse directions using a 31P-nuclear magnetic resonance saturation transfer method. There were no differences in the rate constants or flux rates among the controls, indicating that arginine kinase function is not modulated by salinity if the animal has had sufficient acclimation time. However, the rate constants and flux rates of arginine kinase varied over a modest 1.7-fold range across the three types of osmotic treatments, although the range for the flux data was reduced when cell volume changes were taken into account. The hyperosmotic treatments led to a reduction in arginine kinase flux, while the hypo-osmotic treatments led to an enhanced arginine kinase flux. We propose that this effect is mediated by an increase in the concentration of perturbing inorganic ions under hyperosmotic conditions and a decrease in the concentration of such ions during the hypo-osmotic treatments.

Key words: arginine kinase, osmoregulation, haemolymph, muscle, blue crab, Callinectes sapidus, crustacean, nuclear magnetic resonance, salinity


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   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
J. Exp. Biol.Home page
K. M. Hardy, B. R. Locke, M. Da Silva, and S. T. Kinsey
A reaction-diffusion analysis of energetics in large muscle fibers secondarily evolved for aerobic locomotor function
J. Exp. Biol., September 15, 2006; 209(18): 3610 - 3620.
[Abstract] [Full Text] [PDF]


Home page
J. Exp. Biol.Home page
L. K. Johnson, R. M. Dillaman, D. M. Gay, J. E. Blum, and S. T. Kinsey
Metabolic influences of fiber size in aerobic and anaerobic locomotor muscles of the blue crab, Callinectes sapidus
J. Exp. Biol., November 1, 2004; 207(23): 4045 - 4056.
[Abstract] [Full Text] [PDF]




© The Company of Biologists Ltd 2002