The phosphorylation of intact erythrocytes by exogenously added cAMP-dependent protein kinase

T. M. Chiang, E. S. Kang, Andrew Kang

Research output: Contribution to journalArticle

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Abstract

Intact human erythrocytes incubated with exogenously added cAMP-dependent protein kinase and [γ-32P]ATP resulted in the phosphorylation of several proteins as analyzed by sodium dodecylsulfate-slab gel electrophoresis and radioautography. Bands with apparent molecular weights of 220K, 200K, 180K, 67K, 58K and 29K were phosphorylated by this process. The 220 and 200K components appear to be glycoproteins by their staining characteristics using stain-all. They also precipitate with fibronectin monoclonal antibodies. The identity of the other phosphoproteins is not known. The results indicate that fibronectin and other proteins are substrates for exogenously added cAMP-dependent protein kinase located on the external surfaces of intact human erythrocytes.

Original languageEnglish (US)
Pages (from-to)1446-1452
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume107
Issue number4
DOIs
StatePublished - Aug 31 1982

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Phosphorylation
Cyclic AMP-Dependent Protein Kinases
Fibronectins
Erythrocytes
Phosphoproteins
Electrophoresis
Autoradiography
Precipitates
Glycoproteins
Proteins
Adenosine Triphosphate
Molecular Weight
Gels
Sodium
Molecular weight
Monoclonal Antibodies
Staining and Labeling
Substrates
stains-all

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

The phosphorylation of intact erythrocytes by exogenously added cAMP-dependent protein kinase. / Chiang, T. M.; Kang, E. S.; Kang, Andrew.

In: Biochemical and Biophysical Research Communications, Vol. 107, No. 4, 31.08.1982, p. 1446-1452.

Research output: Contribution to journalArticle

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