Immunological relatedness of the sarcoplasmic reticulum Ca2+-ATPase and the Na+,K+-ATPase

Elek Molnar, Sandor Varga, Istban Jona, Norbert W. Seidler, Anthony Martonosi

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7 Citations (Scopus)


The effect of anti-ATPase antibodies with epitopes near Asp-351 (PR-8), Lys-515 (PR-11) and the ATP binding domain (D12) of the Ca2+-ATPase of sarcoplasmic reticulum (EC was analyzed. The PR-8 and D12 antibodies reacted freely with the Ca2+-ATPase in the native membrane, indicating that their epitopes are exposed on the cytoplasmic surface. Both PR-8 and D12 interfered with the crystallization of the CA2+-ATPase, suggesting that their binding sites are at interfaces between ATPase molecules. PR-11 had no effect on ATPase-ATPase interactions or on the ATPase activity of sarcoplasmic reticulum. The epitope of PR-11 is suggested to be the VIDRC sequence at residues 520-525, while that of D12 at residues 670-720 of the Ca2+-ATPase. The use of predictive algorithms of antigenicity for identification of potential antigenic determinants in the Ca2+-ATPase is analyzed.

Original languageEnglish
Pages (from-to)281-295
Number of pages15
JournalBBA - Biomembranes
Issue number2
Publication statusPublished - Jan 31 1992



  • ATPase, Ca-
  • ATPase, H/K-
  • ATPase, Na/K-
  • Anti-peptide antibody
  • Monoclonal antibody
  • Sarcoplasmic reticulum
  • Transverse tubular membrane

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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