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PMID: 11114023 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Enhancing the intensities of lysine-terminated tryptic peptide ions in matrix-assisted laser desorption/ionization mass spectrometry.

Rapid communications in mass spectrometry : RCM ·Vol. 14 ·No. 23 ·2000-00-00 ·Pages 2147-53

Beardsley RL, Karty JA, Reilly JP

Abstract

Tryptic digests of three proteins are reacted with O-methylisourea in order to convert lysine residues to homoarginines. The resulting homoarginine-terminated peptides exhibit more intense MALDI mass spectral peaks than their lysine-terminated predecessors. This simple chemical reaction should therefore facilitate protein sequencing and mass mapping.

MeSH Terms

Amino Acid Sequence Animals Cattle Databases, Factual Guanine/chemistry Hemoglobins/chemistry,metabolism Humans Lysine/chemistry Methylurea Compounds/chemistry Molecular Sequence Data Peptide Mapping/methods Peptides/analysis,chemistry Serum Albumin, Bovine/chemistry,metabolism Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods Trypsin/chemistry,metabolism

Chemicals

Hemoglobins Methylurea Compounds Peptides O-methylisourea Serum Albumin, Bovine Guanine Trypsin Lysine

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Beardsley R L

Department of Chemistry, Indiana University, Bloomington, IN 47405, USA.

Karty J A

Reilly J P

Article Info

Journal

Rapid communications in mass spectrometry : RCM

Abbr.

Rapid Commun Mass Spectrom

ISSN

0951-4198

DOI

10.1002/1097-0231(20001215)14:23<2147::AID-RCM145>3.0.CO;2-M

Published

2000-00-00

Pages

2147-53

Language

English

Region

England

NLM ID

8802365

Subset

Grants

NIGMS NIH HHS · 1R01 GM6133601 · United States

External Links

PubMed source DOI: 10.1002/1097-0231(20001215)14:23<2147::AID-RCM145>3.0.CO;2-M View journal details

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Enhancing the intensities of lysine-terminated tryptic peptide ions in matrix-assisted laser desorption/ionization mass spectrometry.

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