
The cellular changes that take place as the intestinal cell migrates from crypt to villus are morphologically and biochemically remarkable. It is fortunate that many of these phenomena can be delineated by following enzymic activities. Sucrase-isomaltase is a particularly fascinating enzyme complex because it is a marker of the differentiated cell. Sucrase is inducible with steroids and protected by the substrate sucrose. Purified enzyme can be used to stimulate production of specific antibodies in goats; these antibodies have been used as probes to locate enzymically active and inactive antigen in the cells of the crypt and villus respectively. Further examination of the enzyme has indicated a molecular weight of 200 000--350 000. These higher molecular weight components are located in the brush border of the enterocytes. Lower molecular weight subunits are antigenically active and are in the cytosol. It is assumed that these smaller components are enzymically inactive pre-combination subunits of the sucrase-isomaltase complex and that the sucrase-isomaltase of the brush border is an aggregate of these subunits. The California sea lion, which is deficient in intestinal sucrase activity, does have isomaltase activity. This finding supports the concept that there are different gene complexes for sucrase and for isomaltase.
Aging, Hydrocortisone, Microvilli, Cell Membrane, Fluorescent Antibody Technique, Rats, Sucrase-Isomaltase Complex, Molecular Weight, Kinetics, Multienzyme Complexes, Intestine, Small, Animals, Rabbits, Intestinal Mucosa, Sucrase
Aging, Hydrocortisone, Microvilli, Cell Membrane, Fluorescent Antibody Technique, Rats, Sucrase-Isomaltase Complex, Molecular Weight, Kinetics, Multienzyme Complexes, Intestine, Small, Animals, Rabbits, Intestinal Mucosa, Sucrase
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