Substrate-affinity relationship of succinate dehydrogenase in brain of albino rat during dieldrin toxicity

Substrate kinetics of succinate dehydrogenase (EC 1.3.99.1) were studied in the brain of control and dieldrin-treated albino rats. Dieldrin inhibited the enzyme activity to various degrees and also altered the Michaelis-Menten constant (Km) of the enzyme. Activation energy values (delta E) were incr...

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Bibliographic Details
Published inEcotoxicology and environmental safety Vol. 18; no. 2; p. 141
Main Authors Reddy, G R, Babu, G R, Reddanna, P, Chetty, C S
Format Journal Article
LanguageEnglish
Published Netherlands 01.10.1989
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Summary:Substrate kinetics of succinate dehydrogenase (EC 1.3.99.1) were studied in the brain of control and dieldrin-treated albino rats. Dieldrin inhibited the enzyme activity to various degrees and also altered the Michaelis-Menten constant (Km) of the enzyme. Activation energy values (delta E) were increased, suggesting decreased maximal velocity Vmax, and the high Km obtained for the enzyme also revealed decreased enzyme-substrate affinity and masking of active sites by dieldrin.
ISSN:0147-6513
DOI:10.1016/0147-6513(89)90074-2