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In vitro kinetics of the rat brain succinate dehydrogenase inhibition by hexachlorophene
Author(s) -
Lokanatha V.,
Sailaja P.,
Rajendra W.
Publication year - 1999
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/(sici)1099-0461(1999)13:6<303::aid-jbt3>3.0.co;2-3
Subject(s) - kinetics , in vitro , succinate dehydrogenase , chemistry , hexachlorophene , enzyme kinetics , biochemistry , enzyme , organic chemistry , physics , quantum mechanics , active site
Brain succinate dehydrogenase (SDH) activity was inhibited by in vitro hexachlorophene (HCP) with a half inhibitory concentration (IC 50 ) of 0.65 × 10 −3 M. The HCP exerted noncompetitive inhibition at 0.5 mM (IC 50 ) on SDH activity. The brain SDH demands more energy of activation (ΔE) in the presence of HCP. The ionizable groups of SDH such as the sulfhydral group of cysteine and α‐amino groups of cysteine were not altered qualitatively in the presence of HCP. © 1999 John Wiley & Sons, Inc. J Biochem Toxicol 13: 303–306, 1999