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The classical view of digestion holds that proteins and polypeptides are completely broken down to individual amino acids before absorption from gastrointestinal tract. Little information has been available concerning absorption of peptides. It is known that γ-globulin and some polypeptides can be absorbed without any enzymatic degradation from intestinal mucosa of neonatal animals but not in adult ones. In recent years, some workers (Agar et al., Newey et al., Wiggans et al.) observed absorption of small peptides in animal preparations. Further studies revealed that some protein hormone such as insulin and proteolytic enzymes can be absorbed in its natural form, and the latter are now used orally in certain patients with considerable effect. It is of great interest to elucidate the mechanism of transport of peptide by the intestine. This study is concerned with the absorption of reduced form 35S-GLUTATHIONE (γ-L-Glutamyl-L-Cysteinyl-Glycine, GSH) from rat intestine in vitro and in vivo and the incorporation of the label into protein.

ABSORPTION OF 35S-GSH AND ITS INCORPORATION INTO PROTEIN IN RATS