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Mass spectrometric identification of phosphorylated vasostatin II, a chromogranin A-derived protein fragment (1–113)

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
0167-4838
Publisher
Elsevier
Publication Date
Volume
1343
Issue
2
Identifiers
DOI: 10.1016/s0167-4838(97)00137-4
Keywords
  • Vasostatin Ii
  • Chromogranin A
  • Phosphorylation
  • Electrospray Mass Spectrometry
Disciplines
  • Biology

Abstract

Abstract Vasostatin II, an N-terminal chromogranin A-derived protein (CGA 1–113), was purified from bovine chromaffin granule lysate and characterized by electrospray mass spectrometry (ES/MS) as being partially phosphorylated. The phosphorylation site was determined to be at the Ser 81 position by mass spectrometric peptide mapping and tandem mass spectrometric analysis. This phosphorylation site is close to the processing site (…QKK 78HSS 81 p…) yielding vasostatin I, an N-terminal CGA-derived peptide comprising residues 1–76, suggesting that phosphorylation at Ser 81 is involved in the formation of vasostatin I in chromaffin cells.

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