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Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry of Sialylated Glycopeptides and Proteins Using 2,6-Dihydroxyacetophenone as a Matrix

✍ Scribed by James J. Pitt; Jeffrey J. Gorman

Publisher: John Wiley and Sons
Year: 1996
Tongue: English
Weight: 313 KB
Volume: 10
Category: Article
ISSN: 0951-4198
DOI: 10.1002/(sici)1097-0231(199611)10:14<1786::aid-rcm751>3.0.co;2-i

No coin nor oath required. For personal study only.

✦ Synopsis

A comparison has been performed between 2,6-dihydroxyacetophenone (DHAP) containing di-ammonium hydrogen citrate (DAHC), dihydroxybenzoic acid and a-cyano-4-hydroxycinnamic acid as matrices for matrixassisted laser desorption/ionization (MALDI) of sialylated glycopeptides. DHAP/DAHC was found to yield distinct protonated molecules of large sialylated fetuin tryptic peptides by MALDI-linear time-of-flight analyses. By comparison, the other two matrices produced substantially broadened molecular ion envelopes and indications of considerable in-source and post-source fragmentation. Reflector mode analysis revealed protonated molecules for these peptides in addition to discrete successive post-source fragmentation of sialic acid residues using DHAP/DAHC. The other two matrices produced a much greater degree of fragmentation of sialic acids and failed to reveal the molecular ion in reflector mode. DHAP was also found to be of equivalent efficacy to sinapinic acid for linear mode analysis of bovine serum albumin.

RESULTS AND DISCUSSION

MALDI-linear TOF. spectra of a sialylated tryptic glycopeptide of fetuin, using DHAPIDAHC, DHB and CHCA as matrices (Fig. l(a)-(c)), exemplify the advantage of DHAPl

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