Antigenicities of stem bromelain. Contribution of three-dimensional structure and individual amino acid residues.:Contribution of Three-Dimensional Structure and Individual Amino Acid Residues

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  • SASAKI Makoto
    Department of Biochemistry, Nagoya City University School of Medicine
  • TAKEDA Shinya
    Department of Biochemistry, Nagoya City University School of Medicine
  • KATO Taiji
    Department of Biochemistry, Nagoya City University School of Medicine
  • MATSUBA Kazuhisa
    Department of Biochemistry, Nagoya City University School of Medicine

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The contribution of three-dimensional structure and individual amino acid residues to the antigenicities of macromolecular protein was investigated for a thiol protease stem bromelain as antigen. The extent of the participation was demonstrated by a decrease in antigenicity when the enzyme was denatured in 8 M urea before and after reductive cleavage of intrapeptide disulfide bonds or modified in particular amino acid residues. The results showed that the enzyme treated with 8M urea without reductive cleavage of disulfide bonds preserved about 90% of antigenicity to antibodies against native stem bromelain, while the enzyme denatured after the reductive cleavage of disulfide bonds brought about almost 80% disappearance of the antigenicity. Modification of individual amino acid side chains revealed that lysine was the most immunodominant amino acid, showing 2.5% contribution per residue, and tyrosine followed with 1.2%. However, acidic amino acids such as glutamic and aspartic acids were found to be as low as 0.3%, and tryptophan was 0.2%. These data suggest that most of the antigenic determinants of stem bromelain are of the steric conformation in which lysine and/or tyrosine are most frequently involved as immunodominant amino acids.

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