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A M Buko

Publications and source records attributed to A M Buko.

21 records · Page 2Linked to original sources

Peptide studies using a fast atom bombardment high field mass spectrometer and data system. 1--Sample introduction, data acquisition and mass calibration.

Conditions were established for analyzing as little as 5 pmol of an underivatized peptide delivered in a glycerol sample matrix as a thin film onto a gold-plated copper sample stage and then bombarded with xenon fast atoms. Calibration of the fast atom bombardment high field mass spectrometer and data system was achieved using cesium iodide/glycerol as a reference. Calibration at several accelerating potentials permitted a mass range from 393 to 5941 u. Several factors were examined that contribute to the quality of the mass spectrum: components within the glycerol such as other peptides, alkali salts, acid and reducing agents; the nature of the fast atom gas; concentration of the peptide delivered to the sample stage; and the effect of the sample stage and sample matrix on sensitivity.

Angiotensin I↗

Peptide studies using a fast atom bombardment high field mass spectrometer and data system. 3--Negative ionization: mass calibration, data acquisition and structural characterization.

Under negative ionization conditions, nominal mass calibration of the fast bombardment high field mass spectrometer and data system was accomplished using cesium iodide/glycerol as a reference. Mass calibration at --8 kV accelerating potential extends from m/z 387 to m/z 2170 using xenon fast atoms. Negative xenon FAB mass spectra for human angiotensin I and human gastrin I complement their positive fast atom bombardment spectra. Negative xenon fast atom bombardment spectra of underivatized peptides exhibit molecular proton-abstracted ion envelopes and structurally significant fragment ions. Peptide mixture analysis under negative xenon fast atom bombardment reveals peptide molecular ion envelopes of higher relative intensities than under positive xenon fast atom bombardment.

Angiotensin I↗

Sequence analysis of polypeptides by collision activated dissociation on a triple quadrupole mass spectrometer.

A new approach to the direct sequencing of oligopeptides in complex mixtures is described. Mixtures of [2Ho]/[2H3]-N-acetylated and N,O-permethylated peptides are analyzed by collision activate dissociation on a triple quadrupole mass spectrometer using isobutane chemical ionization. Analysis of the collision activated dissociation spectra enables peptide sequences to be deduced. Use of electron capture negative chemical ionization for the sequence analysis of neuropeptides at the picomole level is also described.

Amino Acid Sequence↗