Abstract
Intraluminal digestive enzymes were shown to bind to chick intestinal epithelial surface (glycocalyx). Affinity of the intestinal epithelium for the enzymes decreased in the order, lipase > amylase > protease. The plant hemagglutinins, Con A, phytohemagglutinin, pokeweed mitogen and raw soybean effectively released lipase and amylase from the glycocalyx. Based on specific inhibition of binding by sugars, such as fucose and N-acetylated sugars, lipase and amylase appeared to be bound to blood group antigen-like sugar moieties on the glycocalyx of the microvilli.
Keywords: amylase, lipase, protease, pancreatic hydrolases, hemagglutinins, lectins, intestinal epitheliurn, glycocalyx
Sammanfattning
Tarminnehållets pankreashydrolaser adsorberades på ut- och in-vända (inverterade) tarmsegmenter. När segmenterna eluerades i en serie provrör med buffrade koksaltlösningar, frigjordes den proteoly-tiska aktiviteten lättare än den amylolytiska eller lipolytiska aktiviteten. Rangordningen för affiniteten måste därför vara: lipas > amylas > proteas.
För att påvisa, att den epiteliala adsorptionen av pankreashydrolaser är en specifik process, gjordes försök att förhindra adsorptionen eller att frigöra den adsorberade enzymaktiviteten med olika sockerarter (som finns i den normala epiteliala kolhydratsubstansen, glycocalyx). Fucos och N-acetylerade sockerarter frigjorde lipas och amylas aktivitet. Växt hemagglutininer, som reagerar med sockerarter på cellytorna, frigjorde effektivt enzymaktivitetet.
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References
- Bennett G, Le Blond C P. Formation of cell coat material for the whole surface of columnar cells in the rat small intestine, as visualized by autoradiography with fucose-3H. J. Cell Biol. 1970;46:409–416. doi: 10.1083/jcb.46.2.409. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brady P G, Vannier A M, Banwell J G. Identification of dietary lectin, wheat germ agglutinin, in human intestinal contents. Gastroenterology. 1978;75:236–239. doi: 10.1016/0016-5085(78)90409-2. [DOI] [PubMed] [Google Scholar]
- Cohen, E., ed.: Biomedical perspectives of agglutinins of invertebrate and plant origins. Ann, N. Y. Acad. Sci. 1974, 234, 1–412.
- Etzler M E. Use of plant agglutinins in characterization of glycoproteins and glycolipids from mammalian cells. Ann. N. Y. Acad. Sci. 1974;234:260–275. doi: 10.1111/j.1749-6632.1974.tb53038.x. [DOI] [PubMed] [Google Scholar]
- Forstner G C. Surface sugar in the intestine. Amer. J. med. Sci. 1969;258:172–180. doi: 10.1097/00000441-196909000-00004. [DOI] [PubMed] [Google Scholar]
- Ito, S. & J. P. Revel: Autoradiographic studies of the enteric surface coat. In Gastrointestinal Radiation Injury. M. F. Sullivan, ed., Excerpta Medica Foundation, Amsterdam 1968, 27–41.
- Jaffe, W. G.: Hemagglutinins. In: Toxic Constituents of Plant Foodstuffs. I. E. Liener, ed., Acad. Press 1969, 69–101.
- Rabat, E. A.: Structural Goncepts in Immunology and Immunochemistry. Holt, Rinehart and Winston, New York, 2nd Ed. 1976.
- Liener I E, Pallansch M J. Purification of a toxic substance from defatted soybean flour. J. biol. Chem. 1952;197:29–36. [PubMed] [Google Scholar]
- Lis, H. & N. Sharon: The biochemistry of plant lectins (phytohemagglutinins). Ann. Rev. Biochem. 1973, 42, 541–574 [DOI] [PubMed]
- Lojda, Z.: Cytochemistry of enterocytes and of other cells in the mucous membrane of the small intestine. In: Biomembranes 4A. D. H. Smyth, ed., Plenum Press, London-New York 1974, 43–122. [PubMed]
- Nitsan Z, Liener I E. Enzymic activities in the pancreas, digestive tract and feces of rats fed raw or heated soy flour. J. Nutr. 1976;106:300–305. doi: 10.1093/jn/106.2.300. [DOI] [PubMed] [Google Scholar]
- Sumner J B, Howell S F. The identification of the hemagglutinins of the jack bean with concanavalin A. J. Bact. 1936;32:227–237. doi: 10.1128/JB.32.2.227-237.1936. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ugolev, A. M.: Membrane (contact) digestion. In: Biomembranes 4A. D. H. Smyth, ed. Plenum Press, London-New York 1973, 285–362. [PubMed]
