Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Helen A. Korsmo"'
Publikováno v:
Gastroenterology. 112:803-812
BACKGROUND & AIMS: Sucrase-isomaltase and lactase-phlorizin hydrolase expressions change remarkably during postnatal development in rats. The aim of this study was to explore the role of transacting nuclear proteins, proteins that bind to the SIF1 ci
Publikováno v:
Pediatric Research. 39:877-881
Despite extensive study in both humans and nonhuman mammals the mechanisms which regulate intestinal lactase activity, particularly during development, are incompletely understood. Our previous studies of human adults are consistent with an important
Publikováno v:
The Journal of clinical investigation. 86(4)
The intestinal brush-border enzyme lactase splits lactose into its component monosaccharides, glucose and galactose. Relative deficiency of the enzyme during adulthood is a common condition worldwide and is frequently associated with symptoms of lact
Publikováno v:
Journal of Clinical Investigation. 65:1174-1181
Past investigation has revealed that the circadian rhythm of intestinal sucrase activity in rats is primarily cued by the time of feeding. We examined the mechanism of the circadian rhythm by methods involving quantitative immunoprecipitation of sucr
Autor:
Helen A. Korsmo, Ward A. Olsen
Publikováno v:
Journal of Clinical Investigation. 60:181-188
Diabetes stimulates the functional activity of the intestinal brush border membrane with enhancement of both hydrolytic enzyme activity and membrane transport systems. To determine the mechanism of this effect, we studied the effects of streptozotoci
Publikováno v:
Metabolism: clinical and experimental. 32(11)
In experimental diabetes, a number of intestinal brush-border hydrolases and transport systems are stimulated. In this study, we assessed possible effects of diabetes on the composition and membrane fluidity of rat intestinal brush-border membranes t
Publikováno v:
Gastroenterology. 92(1)
We used immune electron microscopy to study the intracellular localization of sucrase-isomaltase, an intrinsic glycoprotein of the brush border membrane, to provide insight regarding the sites of its synthesis and intracellular processing and the mec