Availability to monoclonal antibodies of antigenic sites of the alpha and beta subunits in active, denatured or membrane-bound mitochondrial F sub(1)-ATPase

The binding of five monoclonal antibodies to mitochondrial F sub(1)-ATPase has been studied. Competition experiments between monoclonal antibodies demonstrate that these antibodies recognize four different antigenic sites and provide information on the proximity of these sites. The accessibility of...

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Bibliographic Details
Published inBiochimica et biophysica acta, Protein structure and molecular enzymology Vol. 890; no. 1; pp. 55 - 65
Main Authors Moradi-Ameli, M, Godinot, C
Format Journal Article
LanguageEnglish
Published 01.01.1987
Subjects
adenosinetriphosphatase
heart
mitochondria
monoclonal antibodies
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Summary:The binding of five monoclonal antibodies to mitochondrial F sub(1)-ATPase has been studied. Competition experiments between monoclonal antibodies demonstrate that these antibodies recognize four different antigenic sites and provide information on the proximity of these sites. The accessibility of the epitopes has been compared for F sub(1) integrated in the mitochondrial membrane, for purified beta -subunit and for purified F sub(1) maintained in its active form by the presence of nucleotides or inactivated either by dilution in the absence of ATP or by urea treatment. The three anti- beta monoclonal antibodies bound more easily to the beta -subunit than to active F sub(1), and recognized equally active F sub(1) and F sub(1) integrated in the membrane.
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SourceType-Scholarly Journals-1
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ISSN:0167-4838