GLUTATHIONE AS A MATRIX FOR PLASMA DESORPTION MASS SPECTROMETRY OF LARGE PEPTIDES.

Mehrshid Alai, Plamen Demirev, Catherine Fenselau, Robert J. Cotter

Research output: Contribution to journalArticle

Abstract

The plasma desorption mass spectra of large peptides, dissolved and electrosprayed in solutions containing glutathione, showed increased molecular ion signal, reduction of base-line noise and peak widths, and an increase in multiply charged ions. The reduced, rather than the oxidized, form of glutathione is responsible for these effects. Some other chemically similar matrices showed similar effects while others do not. Several roles for the matrix are suggested including previously reported effects on protein refolding and aggregation in solution, as well as possibilities for lowering the sample/substrate binding energy during desorption.

Original languageEnglish (US)
Pages (from-to)1303-1307
Number of pages5
JournalAnalytical Chemistry
Volume58
Issue number7
StatePublished - Jun 1986

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Mass spectrometry
Glutathione
Desorption
Ions
Plasmas
Peptides
Binding energy
Agglomeration
Substrates
Proteins

ASJC Scopus subject areas

  • Analytical Chemistry

Cite this

GLUTATHIONE AS A MATRIX FOR PLASMA DESORPTION MASS SPECTROMETRY OF LARGE PEPTIDES. / Alai, Mehrshid; Demirev, Plamen; Fenselau, Catherine; Cotter, Robert J.

In: Analytical Chemistry, Vol. 58, No. 7, 06.1986, p. 1303-1307.

Research output: Contribution to journalArticle

Alai, Mehrshid ; Demirev, Plamen ; Fenselau, Catherine ; Cotter, Robert J. / GLUTATHIONE AS A MATRIX FOR PLASMA DESORPTION MASS SPECTROMETRY OF LARGE PEPTIDES. In: Analytical Chemistry. 1986 ; Vol. 58, No. 7. pp. 1303-1307.
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