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

Year: 1986

Type: article

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 beta-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.

Source: FEBS Letters

DOI: 10.1016/0014-5793(86)81388-6

Authors: Helmut E. Meyer, Edeltraut Hoffmann-Posorske, Horst Korte, Ludwig M.G. Heilmeyer

Institution: Ruhr University Bochum

Language: English

Topic: Advanced Proteomics Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: bronze

Funder: Deutsche Forschungsgemeinschaft

OpenAlex ID: W1555247363

FWCI: 10.81

Cites: 13

Cited by: 262

Related to: 10