Beta-Naphthol in Ankylostomiasis
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منابع مشابه
Synchronous-derivative phosphorimetric determination of 1- and 2-naphthol in irrigation water by employing beta-cyclodextrin.
A room-temperature phosphorimetric (RTP) study of the inclusion process between 1- and 2-naphthol, beta-cyclodextrin (beta-CD) and 3-bromo-1-propanol as heavy atom pertuber has been performed. Experimental conditions were optimized for the formation of trimolecular complexes with lifetimes of 10.82 and 9.41 ms for 1- and 2-naphthol, respectively. A synchronous-derivative room-temperature phosph...
متن کاملGlucuronidation of 1-naphthol and excretion into the vein in perfused rat kidney.
UDP-glucuronosyltransferase is expressed in the proximal convoluted tubular cells of rat kidney. Kidney perfusion with a Krebs-Henseleit buffer containing 1-naphthol was performed to estimate the dynamics and disposition of the glucuronide conjugate formed in the epithelial cells of the renal tubules. When 1-naphthol was injected into the renal artery, and the perfusate from the renal vein was ...
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Catalytic behavior of isomorphously substituted B-, Al-, Ga-, and Fe-containing extra-large pore UTL zeolites was investigated in Knoevenagel condensation involving aldehydes, Pechmann condensation of 1-naphthol with ethylacetoacetate, and Prins reaction of β-pinene with formaldehyde and compared with large-pore aluminosilicate zeolite beta and representative Metal-Organic-Frameworks Cu3(BTC)2 ...
متن کاملAn assay for the enzyme N-acetyl-beta-D-glucosaminidase (NAGase) based on electrochemical detection using screen-printed carbon electrodes (SPCEs).
An electrochemical assay for the enzyme N-acetyl-beta-D-glucosaminidase (NAGase) is described, using bare screen-printed carbon electrodes (SPCEs). The enzyme substrate, 1-naphthyl-N-acetyl-beta-D-glucosaminide, was added to the NAGase-containing sample under hydrodynamic conditions and was hydrolysed to 1-naphthol, which was monitored amperometrically at an Eapp of +650 mV versus SCE. A pH stu...
متن کاملHuman and rat liver UDP-glucuronosyltransferases are targets of ketoprofen acylglucuronide.
Acylglucuronides formed from carboxylic acids by UDP-glucuronosyltransferases (UGTs) are electrophilic metabolites able to covalently bind proteins. In this study, we demonstrate the reactivity of the acylglucuronide from the nonsteroidal anti-inflammatory drug, ketoprofen, toward human and rat liver UGTs. Ketoprofen acylglucuronide irreversibly inhibited the glucuronidation of 1-naphthol and 2...
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