A monoclonal antibody recognizes a phosphorylated epitope shared by proteins of the cell nucleus and the erythrocyte membrane skeleton.
Monoclonal antibody 3C5 recognizes a family of proteins in the nuclei of cultured cells [(1985) Eur. J. Cell Biol. 38, 344]. This antibody has now been shown to recognize equivalent proteins in liver nuclei and in the Triton-insoluble fraction of tissue extracts. In human erythrocytes the antibody recognized a single protein, present in the membrane skeleton fraction and with the molecular mass and extraction properties of beta-spectrin. The epitope recognized by 3C5 was destroyed by alkaline phosphatase. We conclude that this antibody recognizes a phosphorylation site shared by nuclear proteins and a protein of the erythrocyte membrane skeleton, probably beta-spectrin.
Turner
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BM
Davies
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D000469:Alkaline Phosphatase / Q000494:pharmacology; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D002467:Cell Nucleus / Q000276:immunology*; D002478:Cells, Cultured; D000939:Epitopes / Q000276:immunology*; D004910:Erythrocyte Membrane / Q000276:immunology*; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D010750:Phosphoproteins / Q000276:immunology*; D010766:Phosphorylation; D051381:Rats; D013049:Spectrin / Q000276:immunology
D000911:Antibodies, Monoclonal; D000939:Epitopes; D010750:Phosphoproteins; D013049:Spectrin; D000469:Alkaline Phosphatase