Incomplete intracellular forms of intestinal surface membrane sucrase-isomaltase.

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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...

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Localization of intestinal sucrase-isomaltase complex on the microvillous membrane by electron microscopy using nonlabeled antibodies

Microvillous vesicles isolated from rabbit small intestine showed a trilaminar membrane with a rather smooth surface, which was apparently not affected by papain solubilizing sucrase-isomaltase complex or by trypsin unable to solubilize it. When microvilous vesicles or trysinized ones were incubated with immunoglobulin G against the sucrase-isomaltase complex or monovalent fragments therefrom, ...

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Anchoring 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...

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The 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...

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Topology 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...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1979

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)86796-0