Pesticide used to destroy unwanted vegetation, especially various types of weeds, grasses (POACEAE), and woody plants. Acts by interfering with ATP production. Some plants develop resistance. The active ingredient is no longer contained in any registered pesticide products
Title: Human xenobiotic metabolizing esterases in liver and blood McCracken NW, Blain PG, Williams FM Ref: Biochemical Pharmacology, 46:1125, 1993 : PubMed
Esterases in human liver microsomes hydrolysed fluazifop-butyl (Vmax 9.8 +/- 1.6 mumol/min/g tissue), paraoxon (Vmax 47.4 +/- 7.5 nmol/min/g tissue) and phenylacetate (Vmax 57 +/- 8 mumol/min/g tissue), whereas esterases found in the human liver cytosol hydrolysed fluazifop-butyl (Vmax 10.0 +/- 0.5 mumol/min/g tissue) and phenylacetate (Vmax 37 +/- 2.9 mumol/min/g tissue) but not paraoxon. Human plasma esterase hydrolysed fluazifop-butyl (Vmax 0.09 +/- 0.006 mumol/min/mL), paraoxon (Vmax 210 +/- 14 nmol/min/mL) and phenylacetate (Vmax 250 +/- 17 mumol/min/mL). Inhibitory studies using paraoxon, bis-nitrophenol phosphate and mercuric chloride indicated fluazifop-butyl hydrolysis involved carboxylesterase in liver microsomes and cytosol, and cholinesterase and carboxylesterase in plasma. Phenylacetate hydrolysis involved arylesterase in plasma, both arylesterase and carboxylesterase in liver microsomes and carboxylesterase in liver cytosol. Plasma hydrolysis is less important and overall esterase activity is lower in humans than in the rat which is therefore a poor model.
Title: Peripheral esterases in the rat: effects of classical inducers McCracken NW, Blain PG, Williams FM Ref: Chemico-Biological Interactions, 87:183, 1993 : PubMed
Liver microsomal paraoxonase, aryl esterase and fluazifop butyl esterase (carboxylesterase) were induced by pretreatment of rat with phenobarbitone but not by beta-naphthoflavone or clofibric acid. In the extrahepatic tissues lung cytosolicfluazifop butyl and phenylacetate esterase were induced.
Hydrolysis of acetylsalicylate, benorylate, phenetsal, fluazifop butyl and paraoxon has been studied with freshly isolated rat hepatocytes maintained as a monolayer. Acetylsalicylate and paraoxon were the poorest substrates for hydrolysis whereas benorylate was hydrolysed one hundred times faster. Phenetsal and fluazifop butyl were both hydrolysed at one-tenth of the rate of benorylate. Inhibitor studies with paraoxon, BNPP and physostigmine indicated the involvement of different carboxylesterase isozymes. Studies with acetylsalicylate indicated that uptake of the substrate into the hepatocyte may influence the rate of formation of the hydrolysis product. Studies of hydrolysis in hepatocytes more closely reflect in vivo hepatic hydrolysis than subcellular fractions as cytosolic and microsomal esterases can act in parallel.
