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Journal of Protein Chemistry

, Volume 5, Issue 6, pp 379–384 | Cite as

31P nuclear magnetic resonance study of enzymatically phosphorylated glycophorin A

  • Karen A. Culp
  • Kilian Dill
Article
  • 27 Downloads

Abstract

Glycophorin A was phosphorylated using protein kinases and the new protein was investigated using31P NMR spectroscopy. Most of these ∼30 moles of phosphate were found to be attached to Ser and Thr. Some of these phosphate residues appear to be affected by the carbohydrate residues present. The phosphorylated protein appears to be in a severe state of aggregation, with the degree of aggregationpH-dependent.

Key words

glycophorin A 31P nuclear magnetic resonance spectroscopy phosphorylation phosphoproteins 

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Copyright information

© Plenum Publishing Corporation 1986

Authors and Affiliations

  • Karen A. Culp
    • 1
  • Kilian Dill
    • 1
  1. 1.Department of ChemistryClemson UniversityClemson

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