Antigenic Change of Native and Heat-Denatured Ovalbumin Digested with Pepsin, Trypsin or Chymotrypsin.

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  • 未変性および熱変性オボアルブミンのペプシン, トリプシン, キモトリプシン消化による抗原性の変化
  • Antigenic Change of Native and Heat-Den

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Abstract

Native ovalbumin (NOA) and heat-denatured ovalbumin (HDOA) were digested with pepsin, trypsin or chymotrypsin. The resulting digests were characterized by their degree of hydrolysis, using tricine sodium dodecyl sulfate polyacrylamide gel electrophoresis (tricine SDS-PAGE), and by their degree of antigenicity, namely their binding activity to the anti-NOA rabbit IgG antibody, using an enzyme-linked immunosorbent assay (ELISA). When NOA was digested with pepsin, the degree of hydrolysis increased with the time of incubation (0, 10 and 30 min, and 1, 2, 3, 10 and 24 h); that is, large peptides of MW 45, 000-18, 000 were decreased and small peptides of MW 15, 000-2, 500 were increased. The antigenicity of the NOA digest after 24 h of incubation with pepsin was reduced to 70.9 % of that of intact NOA; however, NOA was barely hydrolyzed with trypsin or chymotrypsin, the antigenicity of the digest remaining almost unchanged. The antigenicity of HDOA, which was obtained by heating a 0.2% NOA solution at pH 7.2 for 10 min at 98 °C, decreased to 81.8 % of that of NOA. The hydrolysis of HDOA was considerably increased and the antigenicity was decreased (i.e., 8.4%, 82.0% and 21.3% in the 24-h digest with pepsin, trypsin and chymotrypsin, respectively). These results indicate that the antigenic structure of ovalbumin is relatively stable.

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