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Analysis of acetylcholine receptor phosphorylation sites using antibodies to synthetic peptides and monoclonal antibodies.

1986; Springer Nature; Volume: 5; Issue: 12 Linguagem: Inglês

10.1002/j.1460-2075.1986.tb04626.x

1460-2075

Anat Safran, Drorit Neumann, Sara Fuchs,

Monoclonal and Polyclonal Antibodies Research

Research Article1 December 1986free access Analysis of acetylcholine receptor phosphorylation sites using antibodies to synthetic peptides and monoclonal antibodies. A. Safran A. Safran Search for more papers by this author D. Neumann D. Neumann Search for more papers by this author S. Fuchs S. Fuchs Search for more papers by this author A. Safran A. Safran Search for more papers by this author D. Neumann D. Neumann Search for more papers by this author S. Fuchs S. Fuchs Search for more papers by this author Author Information A. Safran, D. Neumann and S. Fuchs The EMBO Journal (1986)5:3175-3178https://doi.org/10.1002/j.1460-2075.1986.tb04626.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Three peptides corresponding to residues 354-367, 364-374, 373-387 of the acetylcholine receptor (AChR) delta subunit were synthesized. These peptides represent the proposed phosphorylation sites of the cAMP-dependent protein kinase, the tyrosine-specific protein kinase and the calcium/phospholipid-dependent protein kinase respectively. Using these peptides as substrates for phosphorylation by the catalytic subunit of cAMP-dependent protein kinase it was shown that only peptides 354-367 was phosphorylated whereas the other two were not. These results verify the location of the cAMP-dependent protein kinase phosphorylation site within the AChR delta subunit. Antibodies elicited against these peptides reacted with the delta subunit. The antipeptide antibodies and two monoclonal antibodies (7F2, 5.46) specific for the delta subunit were tested for their binding to non-phosphorylated receptor and to receptor phosphorylated by the catalytic subunit of cAMP-dependent protein kinase. Antibodies to peptide 354-367 were found to react preferentially with non-phosphorylated receptor whereas the two other anti-peptide antibodies bound equally to phosphorylated and non-phosphorylated receptors. Monoclonal antibody 7F2 reacted preferentially with the phosphorylated form of the receptor whereas monoclonal antibody 5.46 did not distinguish between the two forms. Previous ArticleNext Article Volume 5Issue 121 December 1986In this issue RelatedDetailsLoading ...