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Oral bioavailability of proteolytic enzymes
The oral bioavailability of proteolytic enzymes such as e.g. trypsin, chymotrypsin, papain and bromelain has been discussed since their introduction as anti-inflammatory, anti-edematose and immunostimulating agents. The controversy about oral enzyme absorption has not yet been solved, because in the blood proteolytic enzymes bind to antiproteinases and therefore are difficult to quantify with immunological, enzymic and radiochemical methods. Therefore, the amounts of enzymes absorbed in vivo tend to be underestimated (immunological, enzymic methods) or overestimated (radiochemical methods). Quantification as an objective parameter, however, is pivotal for any bioavailability study. Regardless of these analytical difficulties it is presently accepted that proteolytic enzymes when orally administered to man can be detected in the blood plasma, at least to some extent, in their intact, biologically active form. What, however, is still unknown, is the mechanism by which the large molecules cross the intestinal barrier. Using Caco-2 monolayers as a model, some progress was made to better understand this phenomenon. The proteolytic enzymes trypsin, chymotrypsin, papain and bromelain decreased the transepithelial electrical resistance and simultaneously increased the transport of fluorescent marker substances, which normally are not transported across the Caco-2 monolayer. Mucin, albumin and fetal calf serum influence differently the behaviour of these enzymes thus indicating differ
Elsevier Science
ISSN : 0939-6411
European journal of pharmaceutics and biopharmaceutics A. 1996, vol. 42, n° 4, pp. 222-232 [bibl. : 68 ref.]
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