Isoenzyme Spectra of Lactate Dehydrogenase in Organs of Fur-Bearing Animals of Different Ecogenesis

On electrophoretic separation of lactate dehydrogenase (LDH, EC 1.1.1.27) isoenzymes in tissue extracts of heart, kidney, skeletal muscle, and liver in minks, ferrets, polar foxes, foxes, raccoon dogs, nutria, and chinchillas, species peculiarities were revealed in ratios of the agar gel electrophoretic fractions. Thus, a higher relative content of the enzyme A-subunits in the LDH spectra of liver and skeletal muscles was found in semiaquatic animals, minks and nutrias, in comparison with terrestrial animals, polar foxes, ferrets, and chinchillas. In raccoon dogs and chinchillas, a high relative content of the enzyme B-subunits was revealed in these organs. All these data are an example of biochemical specialization of functions at the molecular level to ecological environmental conditions.__________Translated from Zhurnal Evolyutsionnoi Biokhimii i Fiziologii, Vol. 41, No. 3, 2005, pp. 240–246.Original Russian Text Copyright © 2005 by Tyutyunnik, Kozhevnikova, Unzhakov, Meldo.     

Isozyme Patterns of Lactate Dehydrogenase from Tissues of Mink and Arctic Fox during Postnatal Development

Isozymes of lactate dehydrogenase extracted from heart, kidney, and liver of mink (Mustela vison Briss.) and Arctic fox (Alopex lagopus L.) during postnatal development were separated by agarose gel electrophoresis. Tissue-specific isozyme pattern of lactate dehydrogenase can be revealed at the age of one month, while the definitive pattern is formed at the age of four months. The isozyme patterns of lactate dehydrogenase in the studied tissues of mink and Arctic fox share the properties specific for animal species of various ecogenesis.     

Species specificity of the isoenzyme profile of lactate dehydrogenase in organs of rodents of various ecogenesis

Separation of isoenzymes of lactate dehydrogenase (LDH, EC. 1.1.1.27) in extracts of heart, kidney, liver, spleen, lungs of nutrias, chinchillas by agar gel electrophoresis reveals a species specificity in ratio of electrophoretic fractions of the enzyme. The isoenzymes of LDH were seem to play an important role in adaptation of fur animals to environmental conditions. It has been shown that in semiaquatic mammals--nutrias, the relative content of the A-subunits in the isoenzymatic spectrum of LDH in organs was increased as compared with terrestrial animals--chinchillas, whereas relative content of B-subunits in these organs of chinchillas was very high. This is an example of subtle biochemical specialisation of function at molecular level to environmental conditions.     

Lactate dehydrogenase isoenzymes during seasonal adaptations of carnivore fur animals

The seasonal and species-specific peculiarities in the ratio of enzyme electrophoretic fractions are revealed at separation on agar gel plates of lactate dehydrogenase (EC 1.1.1.27) isoenzymes from extracts of the heart, liver, skeletal muscle, and blood serum of minks and polar foxes. The essential role of LDH isoenzymes is revealed in the system of ecological-biochemical adaptations in carnivore fur animals of different ecogenesis. Thus, in amphibionts of the martens family, the minks, in comparison with terrestrial carnivores, the polar foxes, the A-type subunits were characterized by their higher relative contents, while preserving the general organ specificity of the isoenzyme distribution. At the same time, the transition to winter conditions was expressed in the both animal species as an increase of the contents of B-type isoenzymes and a decrease of the anaerobiosis factor. All this confirms the ecological dependence of regulation of metabolism already at the molecular level.     

Lactate dehydrogenase isoenzymes during seasonal adaptations of carnivore fur animals

The seasonal and species-specific peculiarities in the ratio of enzyme electrophoretic fractions are revealed at separation on agar gel plates of lactate dehydrogenase (EC 1.1.1.27) isoenzymes from extracts of the heart, liver, skeletal muscle, and blood serum of minks and polar foxes. The essential role of LDH isoenzymes is revealed in the system of ecological-biochemical adaptations in carnivore fur animals of different ecogenesis. Thus, in amphibionts of the martens family, the minks, in comparison with terrestrial carnivores, the polar foxes, the A-type subunits were characterized by their higher relative contents, while preserving the general organ specificity of the isoenzyme distribution. At the same time, the transition to winter conditions was expressed in the both animal species as an increase of the contents of B-type isoenzymes and a decrease of the anaerobiosis factor. All this confirms the ecological dependence of regulation of metabolism already at the molecular level.     

Isozyme patterns of lactate dehydrogenase from tissues of mink and arctic fox during postnatal development

Isozymes of lactate dehydrogenase extracted from heart, kidney, and liver of mink (Mustela vison Briss.) and Arctic fox (Alopex lagopus L.) during postnatal development were separated by agarose gel electrophoresis. Tissue-specific isozyme pattern of lactate dehydrogenase can be revealed at the age of one month, while the definitive pattern is formed at the age of four months. The isozyme patterns of lactate dehydrogenase in the studied tissues of mink and Arctic fox share the properties specific for animal species of various ecogenesis.