Abstract
Summary 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.
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