PANCREATIC ENZYMES PARTICIPATE IN THE DEGRADATION OF INTESTINAL SUCRASE-ISOMALTASE
نویسندگان
چکیده
منابع مشابه
Incomplete intracellular forms of intestinal surface membrane sucrase-isomaltase.
Sucrase-isomaltase (S-I) is an intestinal membrane enzyme consisting of two active moieties each with its hydrolytic site available for nutrient digestion at the luminal-cell interface. At least 90% of hydrolytic activity can be localized to the brush border membrane and the remainder in the cytoplasm has been considered to originate from brush border contamination. The intracellular cytosol fr...
متن کاملAnchoring and Biosynthesis of Small-Intestinal Sucrase-Isomaltase
The present chapter summarizes some recent and less recent work on the positioning, anchoring and biosynthesis of the small-intestinal sucrase-isomaltase (SI) complex, which is the most abundant integral protein of the brush border membrane; it then discusses the implications of the results as to the possible mechanisms underlying human sucrose-isomaltose malabsorption. I became interested in t...
متن کاملThe clinical consequences of sucrase-isomaltase deficiency
Primary sucrase-isomaltase deficiency, originally thought to be a homozygous recessive disorder, has been found to have numerous genetic variants that alone or in combination (compound heterozygosity) express varying degrees of clinical illness, most commonly causing chronic diarrhea, abdominal pain, and bloating. These symptoms are also present with secondary sucrase-isomaltase deficiency. Rec...
متن کاملTopology and quaternary structure of pro-sucrase/isomaltase and final-form sucrase/isomaltase.
Pig sucrase/isomaltase (EC 3.2.1.48/10) was purified from intestinal microvillar vesicles prepared from animals with and without pancreatic-duct ligation to obtain the single-chain pro form and the proteolytically cleaved final form respectively. The purified enzymes were re-incorporated into phosphatidylcholine vesicles and analysed by electron microscopy after negative staining. The two forms...
متن کاملA probable oxocarbonium ion in the reaction mechanism of small intestinal sucrase and isomaltase.
1-5-D-Gluconolactone is a competitive inhibitor of both sucrase and isomaltase. Substitution of the 1H and 2H at C1 of the glucosyl moiety in p-CL-phenyl-alpha-D-glucopyranoside leads to a decrease in kcat of both sucrase and isomaltase, the k1H/k2H ranging between 1.14 and 1.20. Treatment of the association constants and of the kcat values for a number of p-substituted phenyl-alpha-D-glucopyra...
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ژورنال
عنوان ژورنال: Pediatric Research
سال: 1984
ISSN: 0031-3998,1530-0447
DOI: 10.1203/00006450-198404001-00698