Sequence analysis of phosphoserine‐containing peptides

FEBS Letters

Heilmeyer, Ludwig M.G.¹  Korte, Horst¹  Meyer, Helmut E.¹  Hoffmann-Posorske, Edeltraut¹ 

[1] Institut für Physiologische Chemie, Abteilung für Biochemie Supramolekularer Systeme, Ruhr-Universität Bochum, 4630 Bochum, FRG

关键词: Phosphoserine derivatization;    Sequence analysis;    Phosphopeptide;    S-Ethylcysteine;    S-Ethanolcysteine;    β-Methylaminoalanine;   

DOI  :  10.1016/0014-5793(86)81388-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown