By Prof. Dr. Michael L. G. Gardner, Prof. Dr. Klaus-Jürgen Steffens (auth.)
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Additional info for Absorption of Orally Administered Enzymes
It can be seen that the values in the lymph of these animals are significantly higher than those in the control animals . This is an enzymatic method of identification for amy lase and therefore shows that the functional capabilities of the amylase are still present. Thus, the enzymes are absorbed as complete macromolecules, their functions are still available, and the immunological integrity is also evident. The question is how much of the individual enzymes (pancreatin, trypsin, chymotrypsin, amylase and papain) is actually absorbed.
Pancreatin was absorbed most readily, followed by trypsin and chymotrypsin. Amylase was absorbed easily, but absorption of papain was poorer. It must be realized, however, that the radioactive portion of the radiolabeled molecules, in this case of the enzymes, can be broken off during the process of absorption so that the measured radioactivity may be quantitatively incorrect. Our measurements were performed not only on blood but also on the animal's lymph. Measurements of the lymph were not made continuously but 6 h after administration; this was with the help of lymphatic drainage  and was calculated as the percentage of administered dosage.
Adv Drug Deliv Rev 4:171-207 4. Schilling RJ, Mitra AK (1991) Degradation of insulin by trypsin and alpha-chymotrypsin. Pharm Res 8:721-727 5. Friedman DI, Amidon GL (1991) Oral absorption of peptides: influence of pH and inhibitors on the intestinal hydrolysis of leu-enkephalin and analogues. Pharm Res 8:93-96 6. Parsons JA, Rafferty B, Stevenson RW, Zanelli JM (1977) Use of protease inhibitors to protect subcutaneously injected peptide honnones against local degradation. Br J Pharmacol 59: 489P490P Oral Route of Peptide and Protein Drug Delivery 45 7.
Absorption of Orally Administered Enzymes by Prof. Dr. Michael L. G. Gardner, Prof. Dr. Klaus-Jürgen Steffens (auth.)