Investigation of Digestion and Absorption of a Dietary Protein by Using Its Antigenicity as an Index: Gastrointestinal Digestion of Ovalbuminf

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An attempt was made to use the disappearance of ovalbumin antigen as an index for the analysis of the process of digestion of ovalbumin in vitro and in vivo. The antigenic determinants of ovalbumin were highly sensitive to conformational changes in the protein. Mild heat-treatment and acid-denaturation abolished spontaneously all the reactivities of antigenic determinants. Experiments on protease digestion in vitro showed that native ovalbumin was hardly digested by pepsin at pH 2.7 or by pancreatin at pH 8.0, while acid- or heat-denatured ovalbumin was more easily digested by these proteases. The results suggested that the denaturation of ovalbumin was a rate-limiting step in its digestion, and the disappearance of ovalbumin antigen was a useful index of the initial process of digestion which preceded the proteolytic hydrolysis. At 1 hr after the administration of an ovalbumin diet to rats, approximately 20% of the ovalbumin antigen administered was detected in the whole contents of the gastrointestinal tract. In the small intestine, the amount of intact ovalbumin comprised about half of the total protein of the intestinal contents. These results suggested that in the stomach and small intestine, denaturation of ovalbumin was a significant rate-limiting step in its digestion process. But after 2hr, little ovalbumin antigen was detected in the small intestine. This disappearance of the antigen from the small intestine cannot be well explained by the in vitro data.
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Investigation of Digestion and Absorption of a Dietary Protein by Using Its Antigenicity as an Index: Gastrointestinal Digestion of Ovalbuminf

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