NDLI: Detection and sequencing of phosphopeptides

Content Provider	Springer Nature Link
Author	Zhou, Wei Merrick, B. Alex Khaledi, Morteza G. Tomer, Kenneth B.
Copyright Year	2000
Abstract	Consecutive enzymatic reactions of analytes which are affinity bound to immobilized metal ion beads with subsequent direct analysis of the products by matrix-assisted laser desorption/ ionization mass spectrometry have been used for detecting phosphorylation sites. The usefulness of this method was demonstrated by analyzing two commercially available phosphoproteins, β-casein and α-casein, as well as one phosphopeptide from a kinase reaction mixture. Agarose loaded with either Fe$^{3+}$ or Ga$^{3+}$ was used to isolate phosphopeptides from the protein digest. Results from using either metal ion were complementary. Less overall suppression effect was achieved when Ga$^{3+}$-loaded agarose was used to isolate phosphopeptides. The selectivity for monophosphorylated peptides, however, was better with Fe$^{3+}$-loaded agarose. This technique is easy to use and has the ability to analyze extremely complicated phosphopeptide mixtures. Moreover, it eliminates the need for prior high-performance liquid chromatography separation or radiolabeling, thus greatly simplifying the sample preparation.
Starting Page	273
Ending Page	282
Page Count	10
File Format	PDF
ISSN	10440305
Journal	Journal of The American Society for Mass Spectrometry
Volume Number	11
Issue Number	4
e-ISSN	18791123
Language	English
Publisher	Springer-Verlag
Publisher Date	2000-01-01
Publisher Institution	The American Society for Mass Spectrometry
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Analytical Chemistry Biotechnology Organic Chemistry Proteomics Bioinformatics
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Structural Biology

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Optimized orbitrap HCD for quantitative analysis of phosphopeptides

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Enhanced detection of phosphopeptides in matrix-assisted laser desorption/ionization mass spectrometry using ammonium salts

Quantitation of phosphopeptides using affinity chromatography and stable isotope labeling

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Fragmentation of phosphopeptides by atmospheric pressure MALDI and ESI/ion trap mass spectrometry

Time-resolved observation of product ions generated by 157 nm photodissociation of singly protonated phosphopeptides

The highly selective capture of phosphopeptides by zirconium phosphonate-modified magnetic nanoparticles for phosphoproteome analysis

Detection and sequencing of phosphopeptides

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