|
|
||||||||
AJP - Regulatory, Integrative and Comparative Physiology, Vol 267, Issue 4 1150-R1153, Copyright © 1994 by American Physiological Society
ARTICLES |
J. A. Segal and D. L. Crawford
Department of Organismal Biology and Anatomy, University of Chicago, Illinois 60637.
The temperature-dependent expression of lactate dehydrogenase-B (LDH-B) was compared between two environmentally distinct populations of Fundulus heteroclitus acclimated to 10 degrees C and 20 degrees C. The variability in LDH-B protein expression both within and between populations is consistent with a model of thermal compensation. The northern population from the colder environment expresses a twofold greater amount of LDH-B protein than the warmer southern population at both acclimation temperatures. Correspondingly, both populations have 1.3-fold greater levels of the enzyme at an acclimation temperature of 10 degrees C in comparison to 20 degrees C. In 20 degrees C-acclimated individuals there is a similar twofold difference between populations for LDH-B mRNA concentrations, and LDH-B protein and mRNA are highly correlated (r = 0.81). After acclimation to 10 degrees C, this difference between populations is not seen and in the northern population there is no relationship between LDH-B mRNA and protein levels. Thus the molecular mechanism regulating LDH-B enzyme expression changes in response to temperature acclimation and is different between populations.
This article has been cited by other articles:
![]() |
G. P. Burness, S. C. Leary, P. W. Hochachka, and C. D. Moyes Allometric scaling of RNA, DNA, and enzyme levels: an intraspecific study Am J Physiol Regulatory Integrative Comp Physiol, October 1, 1999; 277(4): R1164 - R1170. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Visit Other APS Journals Online |