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Carbon, hydrogen, nitrogen and chlorine isotope fractionation during 3-chloroaniline transformation in aqueous environments by direct photolysis, TiO photocatalysis and hydrolysis.
Water Res
December 2024
School of Water Resources and Environment and Research Center of Environmental Science and Engineering, Sino-Hungarian Joint Laboratory of Environmental Science and Health, China University of Geosciences (Beijing), 29 Xueyuan Road, Haidian District, 100083 Beijing, China; Department of Technical Biogeochemistry, Helmholtz Centre for Environmental Research-UFZ, Permoserstraße 15 04318 Leipzig, Germany; Isodetect GmbH, Deutscher Platz 5b, 04103 Leipzig, Germany. Electronic address:
This study investigates carbon, hydrogen, nitrogen and chlorine isotope fractionation during the transformation of 3-chloroaniline (3-CA) via direct photolysis, TiO photocatalytic degradation at neutral condition and hydrolysis at pH 3, pH 7 and pH 11. Direct photolysis and ∙OH reaction (UV/HO) showed similar inverse isotope fractionation (ε) for carbon (1.9 ± 0.
View Article and Find Full Text PDFCorrection: H, C, and N resonance assignments of the amyloidogenic peptide SEM2(49-107) by NMR spectroscopy.
Biomol NMR Assign
December 2024
NMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan, 420008, Russia.
NMR resonance assignment of a ligand-binding domain of ephrin receptor A2.
Biomol NMR Assign
December 2024
Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe University, Max-von-Laue-Str. 7, 60438, Frankfurt/Main, Germany.
Ephrin receptors regulate intercellular communication and are thus involved in tumor development. Ephrin receptor A2 (EphA2), in particular, is overexpressed in a variety of cancers and is a proven target for anti-cancer drugs. The N-terminal ligand-binding domain of ephrin receptors is responsible for the recognition of their ligands, ephrins, and is directly involved in receptor activation.
View Article and Find Full Text PDFValidation and Optimization of a Stable Isotope-Labeled Substrate Assay for Measuring AGAT Activity.
Int J Mol Sci
November 2024
Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A1, Canada.
L-arginine: glycine amidinotransferase (AGAT) gained academic interest as the rate-limiting enzyme in creatine biosynthesis and its role in the regulation of creatine homeostasis. Of clinical relevance is the diagnosis of patients with AGAT deficiency but also the potential role of AGAT as therapeutic target for the treatment of another creatine deficiency syndrome, guanidinoacetate N-methyltransferase (GAMT) deficiency. Applying a stable isotope-labeled substrate method, we utilized ARG 15N (ARG-δ2) and GLY 13C15N (GLY-δ3) to determine the rate of 1,2-13C,15N guanidinoacetate (GAA-δ5) formation to assess AGAT activity in various mouse tissue samples and human-derived cells.
View Article and Find Full Text PDFConvenient syntheses of isotopically labeled pyrimidine 2'-deoxynucleosides and their 5-hydroxy oxidation products.
Nucleosides Nucleotides Nucleic Acids
December 2024
Department of Chemistry, Stanford University, Stanford, CA, USA.
Hydrolytic and oxidative damage to pyrimidine nucleobases in DNA represents a significant source of mutations in the human genome. To better understand how these lesions are incorporated and repaired in human cells, it is desirable to have ready access to isotopically enriched nucleosides for use in isotope tracing and mass spectrometry-based quantification experiments. Here we report on improved syntheses of deoxyuridine, deoxycytidine, 5-hydroxydeoxyuridine, and 5-hydroxydeoxycytidine nucleosides labeled with C and N.
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