Sodium trifluoroacetate as a tune/calibration compound for positive- and negative-ion electrospray ionization mass spectrometry in the mass range of 100–4000 Da

Moini, Mehdi; Jones, Bruce L.; Rogers, Robin M.; Jiang, Longfei

doi:10.1016/s1044-0305(98)00079-8

Cited by 102 publications

(82 citation statements)

References 12 publications

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“…Pro39 was dissolved in a mixture of 0.1% trifluoroacetic acid and 50% acetonitrile (1:2) and directly injected into the electrospray ionization mass spectrometer with a syringe pump at a flow rate of 30 l/h. The mass spectrometer was calibrated using sodium trifluoroacetate as described (27). Protein masses were calculated by deconvulation in MassLynx 3.4 (Micromass).…”

Section: Methodsmentioning

confidence: 99%

Site-specific Protease Activity of the Carboxyl-terminal Domain of Semliki Forest Virus Replicase Protein nsP2

Vasiljeva

Valmu

Kääriäinen

et al. 2001

Journal of Biological Chemistry

118

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The virus-specific components (nsP1-nsP4) of Semliki Forest virus RNA polymerase are synthesized as a large polyprotein (P1234), which is cleaved by a virus-encoded protease. Based on mutagenesis studies, nsP2 has been implicated as the protease moiety of P1234. Here, we show that purified nsP2 (799 amino acids) and its C-terminal domain Pro39 (amino acids 459 -799) specifically process P1234 and its cleavage intermediates. Analysis of cleavage products of in vitro synthesized P12, P23, and P34 revealed cleavages at sites 1/2, 2/3, and 3/4. The cleavage regions of P1/2, P2/3, and P3/4 were expressed as thioredoxin fusion proteins (Trx12, Trx23, and Trx34), containing ϳ20 amino acids on each side of the cleavage sites. After exposure of these purified fusion proteins to nsP2 or Pro39, the reaction products were analyzed by SDS-polyacrylamide gel electrophoresis, mass spectrometry, and amino-terminal sequencing. The expected amino termini of nsP2, nsP3, and nsP4 were detected. The cleavage at 3/4 site was most efficient, whereas cleavage at 1/2 site required 5000-fold more of Pro39, and 2/3 site was almost resistant to cleavage. The activity of Pro39 was inhibited by N-ethylmaleimide, Zn 2؉ , and Cu 2؉ , but not by EDTA, phenylmethylsulfonyl fluoride, or pepstatin, in accordance with the thiol proteinase nature of nsP2.

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Section: Methodsmentioning

confidence: 99%

Site-specific Protease Activity of the Carboxyl-terminal Domain of Semliki Forest Virus Replicase Protein nsP2

Vasiljeva

Valmu

Kääriäinen

et al. 2001

Journal of Biological Chemistry

118

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“…Before acquiring the bacterial spectra, the instrument was calibrated using sodium trifluoroacetate [36] such that nominal mass measurement was achieved over the entire mass range (m/z 200 -2000). A mass accuracy of 5-10 ppm was recorded for the standard, at a mass resolution of 4000 FWHM over the acquired mass range.…”

mentioning

confidence: 99%

Flow-injection electrospray ionization mass spectrometry of crude cell extracts for high-throughput bacterial identification

Vaidyanathan

Kell

Goodacre

2002

J. Am. Soc. Mass Spectrom.

101

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Flow-injection electrospray ionization mass spectrometry (FI-ESI-MS) of unfractionated cellfree extracts obtained from bacterial cells suspended in a solvent mixture was investigated as a rapid analytical method for reproducible, high-throughput bacterial identification. Five bacterial strains (two Escherichia coli, two Bacillus spp. and one Brevibacillus laterosporus) were studied in this investigation. Axenically grown bacterial cells were suspended in an acidic organic solvent and the cell-free extract was sequentially injected into a solvent flow stream that was sprayed into the ionization chamber of the ESI-MS. The spectra produced contained reproducible information, which was useful for discriminating between the bacteria. Tandem mass spectrometry was used to characterize further the peaks, and at least three classes of macromolecules, namely phospholipids, glycolipids, and proteins, were found to contribute most to the spectral information. Bacterial extracts stored under different conditions gave very similar mass spectra for each of the five bacterial strains, indicating that the extracts were stable even at room temperature for up to 24 h, with no loss of information content, which has obvious implications for automated high-throughput analysis. An analysis of the components of the extracting solvent mixture and their effects on the spectral information showed that acetonitrile contributes most significantly to the extraction process and hence to the information content of the spectra. (J Am Soc Mass Spectrom 2002, 13, 118 -128)

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“…Calibrate the mass spectrometer using sodium trifluoroacetate 39 . Note: Daily mass calibration can be replaced by this protocol, however, the recommended calibration suggested by the manufacturer should have been completed prior to this calibration.…”

Section: Lc/esi-ms Analysismentioning

confidence: 99%

Improved Polymerase Chain Reaction-restriction Fragment Length Polymorphism Genotyping of Toxic Pufferfish by Liquid Chromatography/Mass Spectrometry

Miyaguchi

2016

JoVE

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An improved version of a polymerase chain reaction (PCR)-restriction fragment length polymorphism (RFLP) method for genotyping toxic pufferfish species by liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS) is described. DNA extraction is carried out using a silica membrane-based DNA extraction kit. After the PCR amplification using a detergent-free PCR buffer, restriction enzymes are added to the solution without purifying the reaction solution. A reverse-phase silica monolith column and a Fourier transform high resolution mass spectrometer having a modified Kingdon trap analyzer are employed for separation and detection, respectively. The mobile phase, consisting of 400 mM 1,1,1,3,3,3-hexafluoro-2-propanol, 15 mM triethylamine (pH 7.9) and methanol, is delivered at a flow rate of 0.4 ml/min. The cycle time for LC/ESI-MS analysis is 8 min including equilibration of the column. Deconvolution software having an isotope distribution model of the oligonucleotide is used to calculate the corresponding monoisotopic mass from the mass spectrum. For analysis of oligonucleotides (range 26-79 nucleotides), mass accuracy was 0.62 ± 0.74 ppm (n = 280) and excellent accuracy and precision were sustained for 180 hr without use of a lock mass standard.

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Sodium trifluoroacetate as a tune/calibration compound for positive- and negative-ion electrospray ionization mass spectrometry in the mass range of 100–4000 Da

Cited by 102 publications

References 12 publications

Site-specific Protease Activity of the Carboxyl-terminal Domain of Semliki Forest Virus Replicase Protein nsP2

Site-specific Protease Activity of the Carboxyl-terminal Domain of Semliki Forest Virus Replicase Protein nsP2

Flow-injection electrospray ionization mass spectrometry of crude cell extracts for high-throughput bacterial identification

Improved Polymerase Chain Reaction-restriction Fragment Length Polymorphism Genotyping of Toxic Pufferfish by Liquid Chromatography/Mass Spectrometry

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