10 research outputs found
In Situ Spectroscopic Studies on the Redox Cycle of NH3−SCR over Cu−CHA Zeolites
The selective catalytic reduction of NO with ammonia (NH3-SCR) catalyzed by Cu-CHA zeolites is thoroughly investigated using in situ spectroscopic experiments combined with on-line mass spectroscopy (MS) under steady-state NH3-SCR conditions and transient conditions for Cu(II)/Cu(I) redox cycles. Quantitative analysis of the in situ XANES spectra of Cu-CHA under steady-state conditions of NH3-SCR show that NH3-coordinated Cu(II) species is the dominant Cu species at low temperatures (100-150 degrees C). At higher temperatures, Cu(II) species and [Cu(NH3)(2)](+) complex coexist, possibly because the rate of the Cu(II) -> Cu(I) reduction step is comparable to that of the Cu(I)-> Cu(II) oxidation step. In situ XANES, IR/MS, and UV-vis/MS experiments on the reduction half cycle demonstrate that the reduction of Cu(II) species occurs via the reaction of NH3-liganded Cu(II) with NO to yield N-2 and H2O. For the oxidation half cycle, in situ XANES experiments of Cu(I) oxidation in 10 % O-2 at 200 degrees C indicate that an increased density in CHA zeolite exhibits a higher oxidation rate. In situ UV-vis experiments of Cu(I) reoxidation using different mixtures of oxidant feed gas demonstrate the key role of O-2 in the oxidation cycle. It is suggested that the reoxidation of Cu(I) to Cu(II) species occurs with only O-2 as the oxidant, and a high Cu density in CHA zeolite promotes SCR activity by enhancing the oxidative activation of Cu(I) to Cu(II) during the catalytic cycle
Toward in Vivo Imaging of Heart Disease Using a Radiolabeled Single-Chain Fv Fragment Targeting Tenascin-C
Toward in Vivo Imaging of Heart Disease Using a Radiolabeled Single-Chain Fv Fragment Targeting Tenascin-C
Antibodies specific to a particular target molecule can be used as analytical reagents, not only for in vitro immunoassays but also for noninvasive in vivo imaging, e.g., immunoscintigraphies. In the latter case, it is important to reduce the size of antibody molecules in order to achieve suitable in vivo "diagnostic kinetics" and generate higher-resolution images. For these purposes, single-chain Fv fragments (scFvs; Mr < 30 kDa) have greater potential than intact immunoglobulins (150 kDa) or Fab (or Fab\u27) fragments (50 kDa). Our recent observation of enhanced tenascin-C (Tnc) expression at sites of cardiac repair after myocardial infarction prompted us to develop a radiolabeled scFv against Tnc for in vivo imaging of heart disease. We cloned the genes encoding the heavy and light chain variable domains of the mouse anti-Tnc monoclonal antibody 4F10, and combined them to create a single gene. The resulting scFv-4F10 gene was expressed in E. coli cells to produce soluble scFv proteins. scFv-4F10 has an affinity for Tnc (Ka = 3.5X107 M–1), similar to the Fab fragment of antibody 4F10 (Ka = 1.3X107 M–1) and high enough to be of practical use. A cysteine residue was then added to the C-terminus to achieve site-specific 111In labeling via a chelating group. The resulting 111In-labeled scFv was administered to a rat model of acute myocardial infarction. Biodistribution and quantitative autoradiographic studies indicated higher uptake of the radioactivity at the infarcted myocardium than the noninfarcted one. Single photon emission computed tomography (SPECT) provided in vivo cardiac images that coincided with the ex vivo observations. Our results will promote advances in diagnostic strategies for heart disease