Search results for "Nitrobenzoates"
showing 6 items of 6 documents
Characterization of (3H) acifluorfen binding to purified pea etioplasts, and evidence that protoporphyrinogen oxidase specifically binds acifluorfen
1992
It is now generally accepted that protoporphyrinogen oxidase is the target-enzyme for diphenylether-type herbicides. Recent studies [Camadro, J-M., Matringe, M., Scalla, R. & Labbe, P. (1991) Biochem. J. 277, 17–21] have revealed that in maize, diphenyl ethers competitively inhibit protoporphyrinogen oxidase with respect to its substrate, protoporphyrinogen IX. In this study, we show that, in purified pea etioplast, [3H]acifluorfen specifically binds to a single class of high-affinity binding sites with an apparent dissociation constant of 6.2 ± 1.3 nM and a maximum density of 29 ± 5 nmol/g protein. [3H]Acifluorfen binding reaches equilibrium in about 1 min at 30°C. Half dissociation occurs…
Gas—liquid chromatographic analyses
1984
Abstract The gas chromatography (GC) of n -alkyl acetates (CH 3 COOR), chloroacetates (CH 2 ClCOOR), dichloroacetates (CHCl 2 COOR) and trichloroacetates (CCl 3 COOR), where the alcohol chain length (R) varied between 1 and 8, and certain of their monochlorinated derivatives, 176 compounds altogether, has been studied on SE-30 and OV-351 glass capillary columns under the same operating conditions. The isomeric monochlorinated esters are eluted in direct order from the 1- chloro to the ω-chloro isomer, the separation of the isomers being complete on OV- 351. On SE-30, however, the peaks of the 6- and 7-chlorooctyl esters are partly overlapped. The separation of the mixtures of odd- and e…
Liquid Chromatographic Analysis of Amphetamine and Related Compounds in Urine Using Solid-Phase Extraction and 3,5-Dinitrobenzoyl Chloride for Deriva…
1997
A chromatographic method for the analysis of amphetamine and related compounds in urine using 3,5-dinitrobenzoyl chloride (3,5-DNB) as a labeling reagent is presented. This assay is based on the employment of solid-phase extraction (SPE) cartridges for sample cleanup and derivatization. Experimental conditions are optimized for the simultaneous derivatization of ephedrine, norephedrine, pseudoephedrine, beta-phenylethylamine, amphetamine, methamphetamine, and 3-phenylpropylamine. The derivatives formed are separated in a LiChrospher 1000 RP18 (125 x 4-mm i.d., 5-microns film thickness) analytical column using a water-acetonitrile gradient elution and detected at 254 nm. Derivatization in C1…
Enhancement of Nitro Reduction in Rat Liver Microsomes by Haemin and Haemoproteins
1978
1. Reductive metabolism of p-nitrobenzoic acid and neoprontosil in rat liver microsomes was studied in the presence of haemin, haemoglobin and myoglobin. 2. Microsomal nitro reduction is enhanced 4-fold in the presence of haemoglobin, whereas azo reduction is not affected. 3. Microsomal nitro reduction is enhanced to a similar extent by haemoglobin, haemin and boiled haemoglobin, whereas myoglobin is about half as active. 4. Maximal enhancement of microsomal nitro reductase activity by haemoglobin is achieved at high substrate concentration (6 mM) and low microsomal protein concentration (0.5--1.0 mg/ml). 5. Control microsomal nitro reduction as well as the haemoglobin-enhanced microsomal n…
Reductive Drug Metabolism in Isolated Perfused Rat Liver under Restricted Oxygen Supply
1978
1. Hepatic azo and nitro reductase activities were studied in the perfused rat liver under normal and restricted oxygen supply. 2. Formation of sulphanilamide or p-aminobenzoic acid from neoprontosil or p-nitrobenzoic acid under aerobic conditions of liver perfusion was negligible, even at a reduced oxygen saturation of a pO2 of 300 mm Hg in the haemoglobinfree perfusion system. At a pO2 of 200 mm Hg reductase activities were almost maximal. 3. Conjugation of sulphanilamide (0-08 mM) was similar under aerobic and anaerobic conditions. Hepatic elimination of p-aminobenzoic acid (0-08 mM) showed an oxygen-dependent increase for 15 min after addition of substrate. 4. p-Nitroanisole demethylati…
Competitive interaction of three peroxidizing herbicides with the binding of 3H acifluorfen to corn etioplast membranes
1990
AbstractThe specific binding of the herbicide acifluorfen 5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid to corn etioplast membranes is competitively inhibited by protoporphyrinogen IX, the substrate of protoporphyrinogen oxidase. Three other peroxidizing molecules, oxadiazon [5-ter-butyl-3-(2,4-dichloro-5-isopropoxyphenyl)-1,3,4-oxadiazol-2-one], LS 82556 [(S)3-N-(methylbenzyl)carbamoyl-5-propionyl-2,6-lutidine], and M&B 39279 [5-amino-4-cyano-1-(2,6-dichloro-4-trifluoromethylphenyl)pyrazol], also compete with acifluorfen for its binding site. The four herbicides thus bind to the same site, or to closely located sites, on the enzyme protoporphyrinogen oxidase.