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In children with CSID, starch digestion correlates well with measures of sucrase activity.
2
Major conclusions: The sucrase and isomaltase domains are closely interacting in the mature protein.
3
The activity of aminopeptidase and sucrase-isomaltase in the test animals was also significantly lower than in the controls.
4
Clinical studies suggest that starch may be poorly digested in those with congenital sucrase-isomaltase deficiency (CSID).
5
Small intestinal breakdown of starch-derived substrates occurs through the mechanisms of small intestinal brush border enzymes, maltase-glucoamylase and sucrase-isomaltase.
6
Control subjects consisted of healthy family members and a group of children with functional abdominal pain with biopsy-proven sucrase sufficiency.
7
General significance: There has been little experimental evidence previously of the effects on activity of interactions between the sucrase-isomaltase enzyme domains.
8
Sterol absorption in intact enterocytes parallels the absorption measured in BBMV, provided that both model systems are normalized to equal sucrase activity.
9
For example, the enzyme that breaks down sucrose (table sugar) is called sucrase; cellulose (plant starch) is broken down by cellulase.
10
Mutational analysis provided evidence that these residues in isomaltase can also affect activity in the partner sucrase domain, suggesting a close interaction between the domains.
11
Sucrase deficiency was previously documented in study subjects by both duodenal biopsy enzyme assays and C-sucrose BT.