Related ArticlesIn vivo detection and characterization of protein adducts resulting from bioactivation of haloethene cysteine S-conjugates by 19F NMR: chlorotrifluoroethene and tetrafluoroethene.
Chem Res Toxicol. 1992 Jan-Feb;5(1):34-41
Authors: Harris JW, Dekant W, Anders MW
Several haloalkenes are selective nephrotoxins. The bioactivation of nephrotoxic haloalkenes involves hepatic glutathione S-conjugate formation, peptidase-catalyzed metabolism of the glutathione S-conjugates to the corresponding cysteine S-conjugates, uptake of cysteine S-conjugates by the kidneys, and renal cysteine conjugate beta-lyase-catalyzed beta-elimination of a thiol. The haloalkyl and haloalkenyl thiols thus released are unstable and yield reactive intermediates whose interactions with cellular constituents are though to contribute to the observed toxicity of S-conjugates. Tetrafluoroethene and chlorotrifluoroethene are metabolized to the cysteine S-conjugates S-(1,1,2,2-tetrafluoroethyl)-L-cysteine (TFEC) and S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine (CTFC), respectively. Administration of TFEC (1.0 mmol/kg) or CTFC (1.0 mmol/kg) to rats resulted in acylation of renal proteins, as demonstrated with 19F nuclear magnetic resonance spectroscopy. Single, broad resonances near 41 or 56 ppm were found in spectra of renal proteins from TFEC- or CTFC-treated rats, respectively, and these resonances were not lost on dialysis. Renal protein incubated with 2-chloro-1,1,2-trifluoroethyl-2-nitrophenyl disulfide, a proreactive intermediate that yields 2-chloro-1,1,2-trifluoroethanethiol, showed the same 19F NMR spectrum as was found with CTFC-treated rats. In vitro incubation of various N alpha-blocked amino acids with this proreactive intermediate indicated that only lysine is stably adducted, whereas histidine is transiently acylated. In each case, proteolysis of modified protein converted a single broad NMR resonance to a doublet with little change in chemical shift and with clearly resolved, characteristic H-F couplings. The single, stable amino acid adduct formed with renal proteins of rats given CTFC or TFEC was N epsilon-(chlorofluorothioacetyl)lysine and N epsilon-(difluorothioacetyl)lysine, respectively.
NMR detection and characterization of sialylated glycoproteins and cell surface polysaccharides
NMR detection and characterization of sialylated glycoproteins and cell surface polysaccharides
Abstract Few solution NMR pulse sequences exist that are explicitly designed to characterize carbohydrates (glycans). This is despite the essential role carbohydrate motifs play in cellā??cell communication, microbial pathogenesis, autoimmune disease progression and cancer metastasis, and despite that fact that glycans, often shed to extra-cellular fluids, can be diagnostic of disease. Here we present a suite of two dimensional coherence experiments to measure three different correlations...
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[NMR paper] 1H and 13C NMR characterization of hemiamidal isoniazid-NAD(H) adducts as possible in
1H and 13C NMR characterization of hemiamidal isoniazid-NAD(H) adducts as possible inhibitors of InhA reductase of Mycobacterium tuberculosis.
Related Articles 1H and 13C NMR characterization of hemiamidal isoniazid-NAD(H) adducts as possible inhibitors of InhA reductase of Mycobacterium tuberculosis.
Chemistry. 2003 May 9;9(9):2034-8
Authors: Broussy S, Coppel Y, Nguyen M, Bernadou J, Meunier B
Isoniazid (INH) is easily oxidized with manganese(III) pyrophosphate, a chemical model of the KatG protein involved in activation of INH inside the...
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[NMR paper] Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectr
Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectroscopy.
Related Articles Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectroscopy.
J Mol Biol. 2002 Sep 13;322(2):425-40
Authors: Rubin SM, Lee SY, Ruiz EJ, Pines A, Wemmer DE
Xenon-binding sites in proteins have led to a number of applications of xenon in biochemical and structural studies. Here we further develop the utility of 129Xe NMR in characterizing specific xenon-protein interactions. The sensitivity of the 129Xe...
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[NMR paper] In vivo detection of the cyclic osmoregulated periplasmic glucan of Ralstonia solanac
In vivo detection of the cyclic osmoregulated periplasmic glucan of Ralstonia solanacearum by high-resolution magic angle spinning NMR.
Related Articles In vivo detection of the cyclic osmoregulated periplasmic glucan of Ralstonia solanacearum by high-resolution magic angle spinning NMR.
J Magn Reson. 2001 Jul;151(1):118-23
Authors: Wieruszeski JM, Bohin A, Bohin JP, Lippens G
We investigate the mobility of the osmoregulated periplasmic glucans of Ralstonia solanacearum in the bacterial periplasm through the use of high-resolution (HR) NMR...
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[NMR paper] NMR and luminescence studies on the formation of ternary adducts between HSA and Ln(I
NMR and luminescence studies on the formation of ternary adducts between HSA and Ln(III)-malonate complexes.
Related Articles NMR and luminescence studies on the formation of ternary adducts between HSA and Ln(III)-malonate complexes.
Biochim Biophys Acta. 1998 Jun 11;1385(1):7-16
Authors: Aime S, Bettinelli M, Ferrari M, Razzano E, Terreno E
At physiological pH and in the presence of an excess of malonate ligand (MAL), the lanthanide ions (Ln=Eu(III), Gd(III) and Tb(III)) are under the form of -. Upon addition of human serum albumin (HSA),...
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[NMR paper] Detection and characterization of an early folding intermediate of T4 lysozyme using
Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR.
Related Articles Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR.
Biochemistry. 1992 May 26;31(20):4749-56
Authors: Lu J, Dahlquist FW
Two-dimensional 1H-15N NMR techniques combined with pulsed hydrogen-deuterium exchange have been used to characterize the folding pathway of T4 lysozyme. In the unfolded state, there is little...
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[NMR paper] Detection and characterization of a folding intermediate in barnase by NMR.
Detection and characterization of a folding intermediate in barnase by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nature.gif Related Articles Detection and characterization of a folding intermediate in barnase by NMR.
Nature. 1990 Aug 2;346(6283):488-90
Authors: Bycroft M, Matouschek A, Kellis JT, Serrano L, Fersht AR
Protein engineering is being developed for mapping the energetics and pathway of protein folding. From kinetic studies on wild-type and mutant proteins, the sequence and energetics of...