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PMID: 2594751 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Fourier-transform mass spectrometry of large molecules by electrospray ionization.

Henry KD, Williams ER, Wang BH, McLafferty FW, Shabanowitz J, Hunt DF

Abstract

The multiply charged ions produced by electrospray ionization of peptides of molecular masses up to 29 kDa have been successfully introduced into a Fourier transform mass spectrometer of unique capabilities for tandem mass spectrometry, large ion dissociation, and resolution. Electrospray ionization places an unusually high number of charges on a peptide yielding mass/charge (m/z) values of 600-1500; in this range at normal operating pressures (approximately 10(-9) torr; 1 torr = 133.3 Pa) Fourier-transform mass spectrometry resolving power is greater than 100,000. Although only 10(-7) torr pressure has been obtained with the initial interface, the resulting resolving power of 5000 makes possible the resolution of isotopic peaks of multiply charged ions. Mass measuring accuracies of a few daltons for molecular masses up to 17 kDa have also been achieved.

MeSH Terms
Enzymes Fourier Analysis Mass Spectrometry/methods Molecular Weight Peptides Proteins
Chemicals
Enzymes Peptides Proteins
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Henry K D
Department of Chemistry, Baker Laboratory, Cornell University, Ithaca, NY 14853.
Williams E R
Wang B H
McLafferty F W
Shabanowitz J
Hunt D F
References (9)
9 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1989-12-00
Pages
9075-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC298436
Subset
IM
Grants
NIGMS NIH HHS · GM-16609 · United States
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