[Radioisotope renographic studies on children with obstruction of the urinary flow in the upper urinary tract].
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Biomedical subjects
Publications and source records attributed to E Kun.
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The cation-complexing carboxylic-acid antibiotic X-537A, at concentrations far below that required for ionophorous activity, selectively inhibits the oxidation of glutamate and isocitrate by liver mitochondria in steady-state 3. The site of inhibition has been localized specifically at the reduction of NADP(+). Glutamate and isocitrate dehydrogenases, the oxidation of NAD(+)-dependent substrates, pyridine nucleotide transhydrogenations, and the respiratory chain between NADH (or NADPH) and O(2) are unaffected by the antibiotic X-537A. Kinetic evidence, i.e., competition between chlorotetracycline (a fluorescence probe for membrane-bound bivalent cation) and X-537A, indicates that the NADP(+)-reducing, antibiotic-sensitive site is most probably associated with the inner mitochondrial membrane.
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The fluorocitrate isomer that is a strong inhibitor and inactivator of aconitase has been shown by x-ray crystallographic studies on the rubidium ammonium salt to have the configurations (1R : 2R) or (1S : 2S) 1-fluoro-2-hydroxy-1,2,3-propanetricarboxylic acid. A possible mechanism for the action of fluorocitrate is proposed which involves the 1R : 2R isomer suggested from biochemical data.