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Am J Physiol Regul Integr Comp Physiol 267: R1150-R1153, 1994;
0363-6119/94 $5.00
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AJP - Regulatory, Integrative and Comparative Physiology, Vol 267, Issue 4 1150-R1153, Copyright © 1994 by American Physiological Society


ARTICLES

LDH-B enzyme expression: the mechanisms of altered gene expression in acclimation and evolutionary adaptation

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.


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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]




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