927 resultados para Polyaniline and derivatives
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Includes bibliographies and index.
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Accompanied by "Supplement ... [to vol. 2-3]" (2 v.) Published: New York, Oxford University Press, 1943.
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Errata slips inserted.
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Mode of access: Internet.
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Vols. 4-5 have imprint: New York, Wiley-Interscience.
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Pages 126 and 127 misnumbered 116 and 117, respectively.
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Mode of access: Internet.
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"Serial no. 110-26."
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References: p. 256-290.
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Tamoxifen is a known hepatocarcinogen in rats and is associated with an increased incidence of endometrial. cancer in patients. One mechanism for these actions is via bioactivation, where reactive metabolites are generated that are capable of binding to DNA or protein. Several metabolites of tamoxifen have been identified that appear to predispose to adduct formation. These include alpha-hydroxytamoxifen, alpha,4-dihydroxytamoxifen, and alpha-hydroxy-N-desmethyltamoxifen. Previous studies have shown that cytochrome P450 (P450) enzymes play an important role in the biotransformation of tamoxifen. The aim of our work was to determine which P450 enzymes were capable of producing a-hydroxylated metabolites from tamoxifen. When tamoxifen (18 or 250,mu M) was used as the substrate, P450 3A4, and to a lesser extent, P450 2D6, P450 2B6, P450 3A5, P450 2C9, and P450 2C19 all produced a metabolite with the same HPLC retention time as alpha-hydroxytamoxifen at either substrate concentration tested. This peak was well-separated from 4-hydroxy-N-desmethyltamoxifen, which eluted substantially later under the chromatographic conditions used. No alpha,4-dihydroxytamoxifen was detected in incubations with any of the forms with tamoxifen as substrate. However, when 4-hydroxytamoxifen (100,mu M) was used as the substrate, P450 2B6, P450 3A4, P450 3A5, P450 1B1, P450 1A1, and P450 2D6 all produced detectable concentrations of a,4-dihydroxytamoxifen. These studies demonstrate that multiple human P450s, including forms found in the endometrium, may generate reactive metabolites in women undergoing tamoxifen therapy, which could subsequently play a role in the development of endometrial cancer.
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The emission from two photoactive 14-membered macrocyclic ligands, 6-((naphthalen-1-ylmethyl)-amino)trans-6,13-dimethyl- 13-amino- 1,4,8,11 -tetraaza-cyclotetradecane (L-1) and 6-((anthracen-9-ylmethyl)-amino)trans-6,13 -dimethyl - 13 -amino- 1,4,8, 1 1-tetraaza-cyclotetradecane (L-2) is strongly quenched by a photoinduced electron transfer (PET) mechanism involving amine lone pairs as electron donors. Time-correlated single photon counting (TCSPC), multiplex transient grating (TG), and fluorescence upconversion (FU) measurements were performed to characterize this quenching mechanism. Upon complexation with the redox inactive metal ion, Zn(II), the emission of the ligands is dramatically altered, with a significant increase in the fluorescence quantum yields due to coordination-induced deactivation of the macrocyclic amine lone pair electron donors. For [ZnL2](2+), the substituted exocyclic amine nitrogen, which is not coordinated to the metal ion, does not quench the fluorescence due to an inductive effect of the proximal divalent metal ion that raises the ionization potential. However, for [ZnL1](2+), the naphthalene chromophore is a sufficiently strong excited-state oxidant for PET quenching to occur.
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The Pd(II) and Pt(II) complexes with triazolopyrimidine C-nucleosides L-1 (5,7-dimethyl-3-(2',3',5'-tri-O-benzoyl-beta-D-ribofuranosyl-s-triazolo)[4,3-a]pyrimidine), L-2 (5,7-dimethyl-3-beta-D-ribofuranosyl-s-triazolo [4,3-a]pyrimidine) and L-3 (5,7-dimethyl[1,5-a]-s-triazolopyrimidine), [Pd(en)(L-1)](NO3)(2), (Pd(bpy)(L-1)](NO3)(2), cis-Pd(L-3)(2)Cl-2, [Pd-2(L-3)(2)Cl-4]center dot H2O, cis-Pd(L-2)(2)Cl-2 and [Pt-3(L-1)(2)Cl-6] were synthesized and characterized by elemental analysis and NMR spectroscopy. The structure of the [Pd-2(L-3)(2)Cl-4]center dot H2O complex was established by Xray crystallography. The two L-3 ligands are found in a head to tail orientation, with a (PdPd)-Pd-... distance of 3.1254(17) angstrom.L-1 coordinates to Pd(II) through N8 and N1 forming polymeric structures. L-2 coordinates to Pd(II) through N8 in acidic solutions (0.1 M HCl) forming complexes of cis-geometry. The Pd(II) coordination to L-2 does not affect the sugar conformation probably due to the high stability of the C-C glycoside bond. (c) 2006 Elsevier B.V. All rights reserved.
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Estimates of microbial crude protein (MCP) production by ruminants, using a method based on the excretion of purine derivatives in urine, require an estimate of the excretion of endogenous purine derivatives (PD) by the animal. Current methods allocate a single value to all cattle. An experiment was carried out to compare the endogenous PD excretion in Bos taurus and high-content B. indicus ( hereafter, B. indicus) cattle. Five Holstein - Friesian ( B. taurus) and 5 Brahman (> 75% B. indicus) steers ( mean liveweight 326 +/- 3.0 kg) were used in a fasting study. Steers were fed a low-quality buffel grass (Cenchrus ciliaris; 59.4 g crude protein/kg dry matter) hay at estimated maintenance requirements for 19 days, after which hay intake was incrementally reduced for 2 days and the steers were fasted for 7 days. The excretion of PD in urine was measured daily for the last 6 days of the fasting period and the mean represented the daily endogenous PD excretion. Excretion of endogenous PD in the urine of B. indicus steers was less than half that of the B. taurus steers ( 190 mu mol/kg W-0.75. day v. 414 mu mol/kg W-0.75. day; combined s.e. 37.2 mu mol/kg W-0.75. day; P< 0.001). It was concluded that the use of a single value for endogenous PD excretion is inappropriate for use in MCP estimations and that subspecies-specific values would improve precision.