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- W2040388680 abstract "Abstract The interaction of the fluorescent hydrophobic probe 1-anilinonaphthalene-8-sulfonate (ANS) with rat hepatic microsomes was examined. The fluorescence of the dye is enhanced about 250-fold and a 45-nm hypsochromic shift occurs in the peak of the ANS emission spectrum. Pretreatment of the rats with phenobarbital or 3-methylcholanthrene, or the reduction of microsomes with sodium dithionite or NADPH did not affect the intensity of fluorescence per mg of microsomal protein. A nonprotein, nonheme, binding locus, probably a phospholipid, is proposed. A Scatchard plot of the ANS conjugate with hepatic microsomes revealed that there is more than one class of binding sites for ANS on microsomes. Several compounds that have been previously shown to be substrates or inhibitors of rat hepatic microsomal NADPH-dependent mixed-function oxidases, modified ANS-microsome fluorescence without altering markedly the microsomal-ANS binding constants. Increases in fluorescence might reflect structural transitions in microsomes. Warfarin, a substrate, appears to displace ANS competitively from a high-affinity binding site without modifying ANS fluorescence due to interaction at a low-affinity binding site. ANS was not found to be a substrate of the hepatic microsomal NADPH-dependent oxidase system, but was an inhibitor of certain microsomal enzymes when added to incubation mixtures in vitro." @default.
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- W2040388680 title "The interaction of a fluorescent probe with rat hepatic microsomes" @default.
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- W2040388680 doi "https://doi.org/10.1016/0009-2797(70)90034-7" @default.
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