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ABSTRACT: Application of developments in the fast atom bombardment ion source and high field magnet technology are presented, which together have resulted in the ability to obtain mass spectra from involatile compounds with molecular weights in excess of 3000 daltons. Examples include resolved molecular species from melittin, glucagon and the oxidized form of the B chain of bovine insulin. It is concluded that there now exists a genuine requirement for extended mass range facilities to be available on a routine basis.
Biological Mass Spectrometry 04/2005; 9(6):265 - 268. · 3.41 Impact Factor
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ABSTRACT: The new technique of fast atom bombardment mass spectrometry has been applied to the investigation of a series of penicillins as free acids or as alkali metal salts. In all cases both positive and negative ion pseudomolecular species are observed giving molecular weight information. Additionally, significant fragmentation is observed in both the positive and negative ion spectra, which gives considerable structural information.
Biological Mass Spectrometry 04/2005; 9(1):11 - 17. · 3.41 Impact Factor
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ABSTRACT: The new technique of fast atom bombardment mass spectrometry has been applied to bradykinin, lysyl-bradykinin and methionyl-lysyl-bradykinin. High sensitivity was obtained at [M + H]+ in the positive ion spectra with a comparable response at [M—H]− in the opposite polarity. All spectra contained an abundance of structurally significant fragment ions. Schemes for relating the observed fragments to the known amino acid sequences are reported for all three molecules. Mass spectrometric investigations on bradykinin were followed by quantitative bioassays which showed that atom bombardment for ten minutes had no measurable effect on the biological activity of microgram samples.
Biological Mass Spectrometry 04/2005; 8(8):337 - 342. · 3.41 Impact Factor
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ABSTRACT: A FAB mapping study of glucagon is described. The absence of important structural information led to a further investigation of the phenomenon. It is suggested that the presence of surface active components in mixtures of peptides can seriously affect the results. It may, in the case of unknown structures, lead to incorrect assignments.
Biological Mass Spectrometry 04/2005; 12(7):355 - 357. · 3.41 Impact Factor
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ABSTRACT: Fast atom bombardment of solids is presented as the basis of a new ion source for mass spectrometry. This novel technique is particularly useful for obtaining mass spectra from involatile and thermally labile materials. The ion source produces both positive and negative ions with equal facility, and examples of both are presented for two underivatized tripeptides. The normal second field free region metastables are observed in a double focusing mass spectrometer and comprehensive metastable pathways have been traced using Barber-Elliott (V-scan) techniques.
Biological Mass Spectrometry 04/2005; 16(6):256 - 260. · 3.41 Impact Factor
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ABSTRACT: Fast atom bombardment mass spectra of a range of involatile mono and disazo sulphonated dyestuffs are presented. Excellent spectra are obtained for dyestuffs containing up to five sulphonate groups. The fragmentations are discussed with special reference to the ions formed by cleavage of the azo linkage. The negative ion spectra are shown to be superior to those obtained in the positive ion mode.
Biological Mass Spectrometry 04/2005; 17(11):569 - 574. · 3.41 Impact Factor
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ABSTRACT: Fast atom bombardment mass spectra of a range of involatile monophosphonated and mixed sulphonated/monophosphonated azo dyestuffs are presented. Good spectra are obtained and the fragmentations are discussed with special reference to the ions formed by cleavage of the azo linkage. The negative ion spectra are shown to be superior in terms of signal to background and structural information to those obtained in the positive ion mode. The results are compared with those obtained from sulphonated azo dyestuffs.
Biological Mass Spectrometry 04/2005; 18(2):75 - 82. · 3.41 Impact Factor
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04/2002;
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Analytical Chemistry 04/1982; 54(4):645A-657A. · 5.86 Impact Factor
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ABSTRACT: We have studied a selection of peptides using a new mass spectrometric ionisation technique - fast atom bombardment (FAB). We define the fragmentation pathways observed and comment on the utility in sequence analysis. A simple acetylation experiment is shown to aid rapid sequence assignment.
Biochemical and Biophysical Research Communications 08/1981; · 2.48 Impact Factor
