Immunochemistry of Bovine Serum Albumin

  • A. F. S. A. Habeeb

Abstract

The molecular basis of protein antigenicity has been of great interest for over three decades, but only very recently has the entire antigenic structure of a protein been determined. So far the antigenic structures of only sperm whale myoglobin and hen egg-white lysozyme have been entirely and precisely determined. The antigenic structure of myoglobin (Atassi, 1975; for a more comprehensive treatment see Atassi, 1977b) comprises five conformationally distinct antigenic sites each made up of six or seven surface amino acid residues that are in direct peptide bond linkage. The recent completion of the entire antigenic structure of lysozyme (Atassi and Habeeb, 1977; Lee and Atassi, 1977a,b; Atassi and Lee, 1978a,b; Atassi, 1978a,b) has revealed that the three antigenic sites of this protein differ from those of myoglobin in a fundamental and fascinating way. Whereas the antigenic sites of myoglobin are composed of residues that are directly linked to one another by peptide bonds, those of lysozyme are each made up of conformationally adjacent surface residues that are not linked directly by peptide bonds but are brought into close proximity by the folding of the protein molecule. These sites react with their respective antibodies as if their residues were in direct peptide bond linkage (Atassi et al., 1976a; Lee and Atassi, 1976). This was unequivocally demonstrated by “surface-simulation” synthesis, a novel and unorthodox approach in which the conformationally adjacent residues constructing the site were linked into a single peptide that did not exist in the protein but attempted to mimic a surface region of it (Atassi et al., 1976a; Lee and Atassi, 1976).

Keywords

Urea Carboxyl Electrophoresis Fractionation Hull 

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Copyright information

© Plenum Press, New York 1979

Authors and Affiliations

  • A. F. S. A. Habeeb
    • 1
  1. 1.Department of Biochemistry and NutritionUniversity of Puerto Rico, Medical Sciences CampusSan JuanPuerto Rico

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