PubMed · 14395448
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
A QUINTON. 1955. Isotopes.. https://pubmed.ncbi.nlm.nih.gov/14395448/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Explore the source record for details and available documents.
High-precision isotope ratio mass spectrometry (IRMS) systems are equipped with digitizers that deliver effective maximum digitization depths of 16 to 24 bits; however, there are no analyses of the proper board depth required to retain high precision in continuous-flow techniques. We report an experimental and theoretical evaluation of quantization error in continuous-flow IRMS (CF-IRMS). CO2 samples (100 pmol-30 nmol) were injected into a gas chromatography combustion IRMS system (GC-CIRMS). The analog signal was digitized by high precision, 24-bit ADC boards at 10 Hz, and was post-processed to simulate 12, 14, and 16-bit data sets. Delta13Cpdh values were calculated for all data sets by the conventional "summation" method or by curve-fitting the chromatographic peaks to the exponentially modified Gaussian (EMG) function. Benchmarks of S.D.(delta13Cpdh) = 0.3, 0.6, and 1.0/1000 were considered to assess precision. In the presence of significant quantization noise, curve-fitting required several-fold less CO2 than the summation method to reach a given benchmark. We derived an equation to describe the theoretical limitations of precision for the summation method as a function of CO2 admitted to the source and the step size of the boards. Theory was in close agreement with the observed lower limit of precision for the simulated 16-bit data set. Curve-fitting achieved a precision of S.D. <0.3/1000 for injections 20-fold smaller than summation for CO2 samples collected on an IRMS with 16-bit resolution. By mitigating the impact of quantization noise, curve-fitting expands the dynamic range within a single run to include lower analyte levels, and effectively reduces the need for high pumping capacities and high precision ADC boards.
A novel MS/MS-based analysis strategy using isotopomer labels, referred to as "tandem mass tags" (TMTs), for the accurate quantification of peptides and proteins is described. The new tags are designed to ensure that identical peptides labeled with different TMTs exactly comigrate in all separations. The tags require novel methods of quantification analysis using tandem mass spectrometry. The new tags and analysis methods allow peptides from different samples to be identified by their relative abundance with greater ease and accuracy than other methods. The new TMTs permit simultaneous determination of both the identity and relative abundances of peptide pairs using a collision induced dissociation (CID)-based analysis method. Relative abundance measurements made in the MS/MS mode using the new tags are accurate and sensitive. Compared to MS-mode measurements, a very high signal-to-noise ratio is achieved with MS/MS based detection. The new tags should be applicable to a wide variety of peptide isolation methods.