๐”– Bobbio Scriptorium
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Malate dehydrogenase isozymes in the longnose dace,Rhinichthys cataractae

โœ Scribed by Ruth M. Starzyk; Robert B. Merritt


Book ID
104784100
Publisher
Springer
Year
1980
Tongue
English
Weight
519 KB
Volume
18
Category
Article
ISSN
0006-2928

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โœฆ Synopsis


The interspecies homology of dace supernatant ( A 2, AB, B2) and mitochondrial (C2) malate dehydrogenase isozymes has been established through cell fractionation a~d 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.


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