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C G Edmonds

Publications and source records attributed to C G Edmonds.

43 records · Page 3Linked to original sources
PubMed1985

Thermospray liquid chromatography-mass spectrometry of nucleosides and of enzymatic hydrolysates of nucleic acids.

Nucleosides dissolved in aqueous buffered solutions undergo ionization during direct introduction of the solution into a mass spectrometer using a thermospray interface. The principal ions formed represent the protonated molecule, the corresponding protonated free base, and sugar. In addition to potential utility for characterization of new nucleosides, the technique can be used to monitor nucleosides separated from enzymatic hydrolysates by liquid chromatography. The selectivity of chromatographic detection is significantly greater than with UV absorbance alone so that independent detection of components of unresolved chromatographic peaks is usually possible. Detection limits, with signal/noise greater than 10 for most nucleosides, are approximately 0.1-1 ng per component for selected ion monitoring and 10-50 ng for full-scan mass spectra. Examples are given from the detection of modified nucleosides in enzymatic hydrolysates of 0.05 A260 units (2.5 micrograms) of rabbit liver tRNAVal and of unfractionated H. volcanii tRNA.

Aerosols↗
PubMed1976

Applications of boronate derivatives in the study of ceramides by gas-liquid chromatography-mass spectrometry.

Methaneboronate derivatives of ceramides possess excellent gas-liquid chromatographic properties and give informative mass spectra. Molecular ions, present at high abundance where an unsaturated acyl substituent is present, are accompanied in the electron impact mass spectra by fragment ions which denote the acyl group and long-chain base. In the gas-liquid chromatographic-mass spectrometric analyses of natural ceramides, as methaneboronate derivatives, the properties of open-tubular columns are exploited to give good separations in moderate analysis times. An application is made to the analysis of ceramides derived from sphingomyelin of human arterial tissue.

Arteries↗
PubMedDate not supplied

Electrospray ionization mass spectrometric characterization of acrylamide adducts to hemoglobin.

The most common procedure to identify hemoglobin adducts has been to cleave the adducts from the protein and characterize the adducting species, by, for example, derivatization and gas chromatography/mass spectrometry. To extend these approaches we used electrospray ionization mass spectrometry (ESI-MS) to characterize adducted hemoglobin. For this we incubated [14C]acrylamide with the purified human hemoglobin (type A0) under conditions that yielded high adduct levels. When the hemoglobin was separated by reversed-phase high-performance liquid chromatography (HPLC), 65% of the radioactivity copurified with the beta-subunit. Three adducted species were prominent in the ESI mass spectrum of the intact beta-subunit, indicating acrylamide adduction (i.e., mass increase of 71 Da) and two additional unidentified moieties with mass increments of 102 and 135 Da. Endoproteinase Glu-C digestion of the adducted beta-subunit resulted in a peptide mixture that, upon reversed-phase HPLC separation, provided several radiolabeled peptides. Using ESI-MS we identified these as the V91-101 and V102-122 peptides that represent the cysteine-containing peptides of the beta-subunit. These results provide definitive information on acrylamide-modified human hemoglobin and demonstrate that ESI-MS provides valuable structural information on chemically adducted proteins.

Acrylamides↗