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Easy amino acid sequencing of sulfonated peptides using post-source decay on a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer equipped with a variable voltage reflector.
Rapid Commun Mass Spectrom. 2002; 16(19):1851-9.RC

Abstract

Tryptic peptides were labeled with sulfonic acid groups at the N-termini using an improved chemistry. The derivatization was performed in common aqueous buffers on peptides adsorbed onto a ZipTip trade mark C(18), thus allowing simultaneous desalting/concentration of the sample. When only Arg-terminating peptides were considered, the procedure from adsorption onto the ZipTip until analysis by MALDI-PSD took about 10 min and several samples could be worked on in parallel. The resulting improved post-source decay (PSD) fragmentation produced spectra containing only y-ions. PSD amino acid sequencing of underivatized and derivatized synthetic peptides was compared. From the sequence information obtained from derivatized peptides isolated by ion selection from tryptic in-gel digests, a protein was correctly identified which was difficult to analyze from an unclear peptide mass fingerprint analysis. The method was also applied to the identification and localization of phosphorylated Ser and Tyr residues in native and synthetic peptides.

Authors+Show Affiliations

Ludwig Institute for Cancer Research, Box 595, SE-751 24 Uppsala, Sweden. ulf.hellman@licr.uu.seNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

12271450

Citation

Hellman, Ulf, and Rama Bhikhabhai. "Easy Amino Acid Sequencing of Sulfonated Peptides Using Post-source Decay On a Matrix-assisted Laser Desorption/ionization Time-of-flight Mass Spectrometer Equipped With a Variable Voltage Reflector." Rapid Communications in Mass Spectrometry : RCM, vol. 16, no. 19, 2002, pp. 1851-9.
Hellman U, Bhikhabhai R. Easy amino acid sequencing of sulfonated peptides using post-source decay on a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer equipped with a variable voltage reflector. Rapid Commun Mass Spectrom. 2002;16(19):1851-9.
Hellman, U., & Bhikhabhai, R. (2002). Easy amino acid sequencing of sulfonated peptides using post-source decay on a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer equipped with a variable voltage reflector. Rapid Communications in Mass Spectrometry : RCM, 16(19), 1851-9.
Hellman U, Bhikhabhai R. Easy Amino Acid Sequencing of Sulfonated Peptides Using Post-source Decay On a Matrix-assisted Laser Desorption/ionization Time-of-flight Mass Spectrometer Equipped With a Variable Voltage Reflector. Rapid Commun Mass Spectrom. 2002;16(19):1851-9. PubMed PMID: 12271450.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Easy amino acid sequencing of sulfonated peptides using post-source decay on a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer equipped with a variable voltage reflector. AU - Hellman,Ulf, AU - Bhikhabhai,Rama, PY - 2002/9/25/pubmed PY - 2002/10/31/medline PY - 2002/9/25/entrez SP - 1851 EP - 9 JF - Rapid communications in mass spectrometry : RCM JO - Rapid Commun Mass Spectrom VL - 16 IS - 19 N2 - Tryptic peptides were labeled with sulfonic acid groups at the N-termini using an improved chemistry. The derivatization was performed in common aqueous buffers on peptides adsorbed onto a ZipTip trade mark C(18), thus allowing simultaneous desalting/concentration of the sample. When only Arg-terminating peptides were considered, the procedure from adsorption onto the ZipTip until analysis by MALDI-PSD took about 10 min and several samples could be worked on in parallel. The resulting improved post-source decay (PSD) fragmentation produced spectra containing only y-ions. PSD amino acid sequencing of underivatized and derivatized synthetic peptides was compared. From the sequence information obtained from derivatized peptides isolated by ion selection from tryptic in-gel digests, a protein was correctly identified which was difficult to analyze from an unclear peptide mass fingerprint analysis. The method was also applied to the identification and localization of phosphorylated Ser and Tyr residues in native and synthetic peptides. SN - 0951-4198 UR - https://www.unboundmedicine.com/medline/citation/12271450/Easy_amino_acid_sequencing_of_sulfonated_peptides_using_post_source_decay_on_a_matrix_assisted_laser_desorption/ionization_time_of_flight_mass_spectrometer_equipped_with_a_variable_voltage_reflector_ L2 - https://doi.org/10.1002/rcm.805 DB - PRIME DP - Unbound Medicine ER -