Mixture of caesium iodide, sodium iodide, and glycerol as a calibrant for routine fast atom bombardment mass analysis.
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چکیده
منابع مشابه
FAST ATOM BOMBARDMENT MASS SPECTROMETRY (FABMS) ANALYSIS OF AN N- TERMINAL - BLOCKED PEPTIDE
FABMS analysis of T-lb peptide before and after one cycle of Edman degradation indicated an unblocked N-terminal Thr residue for this tryptic peptide. In contrast , our data showed a molecular protonated ion, MH + for T- la peptide at 655 mass units (mu) which is 42 mu higher than the MH ion of T- 1b peptide. In addition, T- la peptide was not amenable to one cycle of manual Edman degrada...
متن کاملFast - atom - bombardment mass spectrometry
A detailed study of the mass spectra of peptides produced by the new technique of fast-atom bombardment is reported. Molecular weights of unmodified peptides containing up to 21 amino acids have been determined. In favourable cases, the molecular-weight determination may be made on as little as 0.1 nmol of sample. Positive-ion and negative-ion spectra are obtained with equal facility. With samp...
متن کاملContinuous-flow fast atom bombardment mass spectrometry.
The continuous-flow fast atom bombardment probe performs equally well with or without a high-performance liquid chromatography column producing clean spectra containing little or no background noise. Its function as a liquid chromatography-mass spectrometry interface for labile and involatile samples has been illustrated with reference to dansylated amino acids. The versatility of the new probe...
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14. Barber, M., Bordoli, R. S., Sedgwick, R. D. & ‘lylcr, A. N . ( 198 I ) J. Chem. Soc. Chem. Commirri. 7,325-327 Biemann, K. & Martin, S. A. ( 1 987) Moss Spectrom. Rev. 6 , 1-76 Gibson, B. W. & Biemann, K. (1984) /’roc. Nor/. Aciid. Sci. U.S.A. 8 I , 1956I960 Allmaier, G., Chao, B. H., Khorana, H. G. & Biemann, K. ( 1986) in Annual Conference on Moss Spectrometty w i r l Allied Topics 34h, p...
متن کاملfast atom bombardment mass spectrometry (fabms) analysis of an n- terminal - blocked peptide
fabms analysis of t-lb peptide before and after one cycle of edman degradation indicated an unblocked n-terminal thr residue for this tryptic peptide. in contrast , our data showed a molecular protonated ion, mh + for t- la peptide at 655 mass units (mu) which is 42 mu higher than the mh ion of t- 1b peptide. in addition, t- la peptide was not amenable to one cycle of manual edman degradation. ...
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ژورنال
عنوان ژورنال: Journal of the Mass Spectrometry Society of Japan
سال: 1988
ISSN: 1340-8097,1880-4225
DOI: 10.5702/massspec.36.81