INTESTINAL DIGESTION AND ABSORPTION OF SUGARS AND PEPTIDES.
Rept. no. 4 (Final), 1 Jan 68-28 Feb 69,
ZURICH UNIV (SWITZERLAND) BIOCHEMISCHES INSTITUT
Pagination or Media Count:
Mammalian intestinal sucrase is activated by sodium in different ways in different species. The sodium-activation constants have been determined. Sodium-activation does not follow any compulsory reaction sequence. No diffusion barrier can be detected between lumen and intestinal sucrase. Trehalase also shows a cooperative interaction between substrate sites. It is not activated by sodium. The intestinal sucrase-isomaltase complex can be split into subunits. The intestinal sucrase-isomaltase complex can bind glucose in a manner similar to what one would expect from the substrate site of the sugar transport carrier. With ferritin marked antibodies intestinal sucrase could be located at the membrane of the brush border. Rat intestinal lactase was obtained in an essentially homogeneous form. The anomeric form of the product liberated by a number of digestive carbohydrases was determined. Author
- Anatomy and Physiology