Different Functional and Structural Properties of Lactate Dehydrogenase Isozymes at Different Stages of Danio rerioOntogenesis

Different Functional and Structural Properties of Lactate Dehydrogenase Isozymes at Different... We studied properties of lactate dehydrogenase isozymes expressed at different stages of Danio rerioontogenesis. H4-LDH and a minor fraction H3M1are expressed during embryonic development. The muscle isozyme (Н4) appears after the beginning of muscle contractions in the embryo. Н4and М4isozymes isolated from the heart and skeletal muscle of the adult fish, respectively, show significant differences in terms of Michaelis constant (K m) activation energy (AE), and inactivation temperature. H4-LDH isozymes isolated from unfertilized eggs, the skeletal muscle of larvae, and the heart of the adult fish differ inK mand activation energy, as well as in inactivation temperature. We propose that these differences may be associated with a ligand interacting with the H4isozyme at different steps of ontogenesis. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Developmental Biology Springer Journals

Different Functional and Structural Properties of Lactate Dehydrogenase Isozymes at Different Stages of Danio rerioOntogenesis

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Publisher
Springer Journals
Copyright
Copyright © 2001 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Animal Anatomy / Morphology / Histology
ISSN
1062-3604
eISSN
1608-3326
D.O.I.
10.1023/A:1012360501778
Publisher site
See Article on Publisher Site

Abstract

We studied properties of lactate dehydrogenase isozymes expressed at different stages of Danio rerioontogenesis. H4-LDH and a minor fraction H3M1are expressed during embryonic development. The muscle isozyme (Н4) appears after the beginning of muscle contractions in the embryo. Н4and М4isozymes isolated from the heart and skeletal muscle of the adult fish, respectively, show significant differences in terms of Michaelis constant (K m) activation energy (AE), and inactivation temperature. H4-LDH isozymes isolated from unfertilized eggs, the skeletal muscle of larvae, and the heart of the adult fish differ inK mand activation energy, as well as in inactivation temperature. We propose that these differences may be associated with a ligand interacting with the H4isozyme at different steps of ontogenesis.

Journal

Russian Journal of Developmental BiologySpringer Journals

Published: Oct 9, 2004

References

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