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Literature DB >> 7470020

Malate dehydrogenase isozymes in the longnose dace, Rhinichthys cataractae.

Abstract

The interspecies homology of dace supernatant (A2,AB,B2) and mitochondrial (C2) malate dehydrogenase isozymes has been established through cell fractionation and tissue distribution studies. Isolated supernatant malate dehydrogenase (s-MDH) isozymes show significant differences in Michaelis constants for oxaloacetate and in pH optima. Shifts in s-MDH isozyme pH optima with temperature may result in immediate compensation for increase in ectotherm body pH with decrease in temperature, but duplicate s-MDH isozymes are probably maintained through selection for tissue specific regulation of metabolism.

Entities: Chemical Species

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Year: 1980 PMID： 7470020 DOI： 10.1007/bf00484591

Source DB: PubMed Journal: Biochem Genet ISSN： 0006-2928 Impact factor: 1.890

16 in total

1. Evolution of a gene. Multiple genes for LDH isozymes provide a model of the evolution of gene structure, function and regulation.

Authors: C L Markert; J B Shaklee; G S Whitt
Journal: Science Date: 1975-07-11 Impact factor: 47.728

2. Theoretical analysis of the effects of two pH regulation patterns on the temperature sensitivities of biological systems in nonhomeothermic animals.

Authors: T L Wilson
Journal: Arch Biochem Biophys Date: 1977-08 Impact factor: 4.013

3. Molecular aspects of temperature acclimation in fish: contributions of changes in enzyme activities and isozyme patterns to metabolic reorganization in the green sunfish.

Authors: J B Shaklee; J A Christiansen; B D Sidell; C L Prosser; G S Whitt
Journal: J Exp Zool Date: 1977-07

4. Effects of temperature on the kinetics of malate dehydrogenase from a cold climate reptile, Thamnophis sirtalis parietalis.

Authors: M A Hoskins; M Aleksiuk
Journal: Comp Biochem Physiol B Date: 1973-06-15

1. Thermal kinetic differences between allelic isozymes of malate dehydrogenase (Mdh-B locus) of largemouth bass, Micropterus salmoides.

Authors: S A Hines; D P Philipp; W F Childers; G S Whitt
Journal: Biochem Genet Date: 1983-12 Impact factor: 1.890

1 in total

Malate dehydrogenase isozymes in the longnose dace, Rhinichthys cataractae.

1. Evolution of a gene. Multiple genes for LDH isozymes provide a model of the evolution of gene structure, function and regulation.

2. Theoretical analysis of the effects of two pH regulation patterns on the temperature sensitivities of biological systems in nonhomeothermic animals.

3. Molecular aspects of temperature acclimation in fish: contributions of changes in enzyme activities and isozyme patterns to metabolic reorganization in the green sunfish.

4. Effects of temperature on the kinetics of malate dehydrogenase from a cold climate reptile, Thamnophis sirtalis parietalis.

5. Role of body temperature in determining the acid-base state in vertebrates.

6. Esterase heterogeneity: dynamics of a polymorphism.

7. The molecular basis for isozymes.

8. Loss of duplicate gene expression after polyploidisation.

9. Multiple forms of supernatant malate dehydrogenase in salmonid fishes.

10. GENIC VARIABILITY IN THE LONGNOSE DACE, RHINICHTHYS CATARACTAE.

1. Thermal kinetic differences between allelic isozymes of malate dehydrogenase (Mdh-B locus) of largemouth bass, Micropterus salmoides.