Abstract
The spatial organization and the antigenic structure of the bacteriorhodopsin molecule in the purple membrane were studied by immunochemical techniques. Five monoclonal antibodies directed against exposed parts of the protein molecule in the membrane were prepared and characterized. Antigenic determinants were localized in the bacteriorhodopsin polypeptide chain by analysis of the interaction between monoclonal antibodies and protein fragments. The structure of antigenic determinants was revealed by the interaction of monoclonal antibodies with (i) isolated bacteriorhodopsin fragments further modified by sequential Edman degradation and (ii) derivatives of bacteriorhodopsin obtained biosynthetically or by selective chemical modification. Five antigenic determinants were localized in the following parts of bacteriorhodopsin: < Glu'-Met 20 involving one of the 3 amino acid residues of the N-terminal part; Gly 33-Met 56 involving Asp 36 and/or Asp 38 and Phe 42; Phe 156-Met 163 involving Phe 156; Glu 194-Leu 207 involving Glu 194; Pro 200-Leu 207.
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