0000000000323457

AUTHOR

M. Przybylski

showing 5 related works from this author

Problems of electron detection in Depth-Selective Conversion Electron Mössbauer Spectroscopy

1992

Applications of Depth-Selective Conversion Electron Mossbauer Spectroscopy (DCEMS) are limited by the long measuring times needed for collecting sufficient data statistics. To shorten the recording time, the background should be reduced and the detection efficiency for conversion electrons should be improved. For57Co/57Fe DCEMS, systematic studies were performed to investigate the origin, shape, and structure of the background components in DCEMS data distributions for various samples using channeltrons and low-noise scintillation counters as electron detectors.

PhysicsNuclear and High Energy PhysicsOpticsbusiness.industryConversion electron mössbauer spectroscopyScintillation counterDetectorElectronPhysical and Theoretical ChemistryAtomic physicsCondensed Matter PhysicsbusinessAtomic and Molecular Physics and OpticsHyperfine Interactions
researchProduct

Exopeptidase digestion in combination with field desorption mass spectrometry for amino acid sequence determination

1982

Numerous studies have been devoted in the last years to the development of mass spectrometric methods for the sequence determination of peptides [ 1,2]. Most advanced among this work has been so far the rigorous chemical derivatization of oligopeptides to achieve sufficient volatility for the application of conventional (electron impact, EI) mass spectrometry [2-41. For example, the analysis by gas chromatography-mass spectrometry (GC-MS) of mixtures of oligopeptide fragments derivatized after chemical or enzymatic hydrolysis of polypeptides has been successfully used for sequence determinations [2,5]. Major limitations of this approach are that only small peptide derivatives are amenable t…

Exopeptidase activityChromatographyProtein mass spectrometrybiologyChemistryBiophysicsProteinsCell BiologyExopeptidaseMass spectrometryBiochemistryMass SpectrometrySample preparation in mass spectrometryStructural BiologyField desorptionExopeptidasesGeneticsbiology.proteinMass spectrumAmino Acid SequenceMolecular BiologyPeptide sequencePeptide HydrolasesFEBS Letters
researchProduct

Methods for the rapid detection, isolation and sequence determination of “peptaibols” and other aib-containing peptides of fungal origin. I. Gliodeli…

1984

A rapid and simple detection procedure of Aib-containing “peptaibol” polypeptide antibiotics (mycotoxins) in fungal culture broths is described which employs alkylsilica (Sep-Pak®) cartridges for a selective enrichment, and the utilization of the unusualα-aminoisobutyric acid (Aib) and amino alcohols as specific marker constituents, which are easily detectable in total hydrolysates. Preparative isolations from fermentation broths is facilitated by adsorber resin (XAD) column chromatography, and purification of crude isolates is achieved by silica gel- and sephadex LH-20 chromatography. Preparative HPLC using spherical, totally porous ODS-bonded phases enables the isolation of uniform peptid…

ChromatographyResolution (mass spectrometry)Silica gelOrganic ChemistryClinical BiochemistryPeptaibolFast atom bombardmentMass spectrometryBiochemistryAnalytical ChemistryComplete sequencechemistry.chemical_compoundColumn chromatographychemistrySephadexChromatographia
researchProduct

Chromatographic and mass spectrometric characterization of the structures of the polypeptide antibiotics samarosporin and stilbellin and identity wit…

1983

The structural identity of the polypeptide antibiotics, samarosporin I(II) and stilbellin I(II) with emerimicin IV(III) has been established by thin-layer chromatography, quantitative amino acid analysis by ion-exchange chromatography, gas-liquid chromatography of the N-pentafluoropropionyl amino acid n-propyl esters and N,O-bis-pentafluoropropionyl phenylalaninol with quartz capillaries coated with the chiral stationary phase N-propionyl-L-valine-tert-butylamide, and determination of the relative molecular masses and sequence-specific fragments by field desorption fast atom bombardment mass spectrometry. The separation of closely related sequence analogues of the above polypeptides could b…

chemistry.chemical_classificationAqueous solutionChromatographyChemistryOrganic ChemistryClinical BiochemistryPeptaibolFast atom bombardmentMass spectrometryBiochemistryAnalytical ChemistryAmino acidchemistry.chemical_compoundColumn chromatographyIsovalineMoleculeOrganic chemistryChromatographia
researchProduct

Mass spectral identification of the blocked N-terminal tryptic peptide of the ATPase inhibitor from beef heart mitochondria

1984

AbstractThe presence of a formyl blocking group at the N-terminus of the ATPase inhibitor has been identified and the partial sequence of the N-terminal peptide has been determined by fast atom bombardment and field desorption coupled to mass spectrometry. Minor discrepancies in amino acid sequence of the inhibitor between the present and published data [(1981) Proc. Natl. Acad. Sci. USA 78, 7403-7407] are reported and its relationships with other inhbitors are briefly discussed.

Fast atom bombardmentATPaseBiophysicsPeptideN-formyi blocking groupSaccharomyces cerevisiaeMass spectrometryBiochemistryMass SpectrometryMitochondria HeartSpecies SpecificityStructural BiologyEndopeptidasesGeneticsAnimalsTrypsinAmino Acid SequenceMolecular BiologyPeptide sequencechemistry.chemical_classificationBeef heart mitochondriabiologyChemistryTryptic peptideProteinsCell BiologyFast atom bombardmentField desorption Amino acid sequenceATPase inhibitorPeptide FragmentsMitochondriaProton-Translocating ATPasesBiochemistrybiology.proteinCattleFEBS Letters
researchProduct