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Sequence analysis of phosphoserine‐containing peptides: Modification for picomolar sensitivity

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Meyer, Helmut E., Hoffmann-Posorske, Edeltraut, Korte, Horst, Heilmeyer, Ludwig M.G.·1986·FEBS Letters

Abstract

Sequencing of phosphoserine‐containing peptides yields normally no identifiable PTH‐derivatives at those positions where phosphoserine is located. Here a new method is described which allows identification of the position of phosphoserine by chemical modification just before sequence analysis. In a one‐step microbatch reaction, phosphoserine present in the intact peptide can be transformed quantitatively into stable derivatives such as β‐methylaminoalanine (MAA), S‐ethanolcysteine or S‐ethylcysteine. These derivatives are detectable during microsequencing with less than 100 pmol peptide using an Applied Biosystems gas‐phase sequencer equipped with an on‐line PTH amino acid analyzer.

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Metadata

Authors
Meyer, H. E., Hoffmann-Posorske, E., Korte, H., & Heilmeyer, L. M. G.
Venue
FEBS Letters
Publisher
Wiley
Published
1986-08-11
Volume
204
Issue
1
Pages
61-66
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W1555247363
Cited by
260
References
0
FWCI
10.82
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Sequence analysis of phosphoserine‐containing peptides: Modification for picomolar sensitivity. https://app.cochat.ai/papers/10.1016/0014-5793(86)81388-6
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Meyer, H. E., Hoffmann-Posorske, E., Korte, H., & Heilmeyer, L. M. G. (1986). Sequence analysis of phosphoserine‐containing peptides: Modification for picomolar sensitivity. FEBS Letters. https://doi.org/10.1016/0014-5793(86)81388-6

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