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 کاملSmall intestinal sucrase and isomaltase split the bond between glucosyl-C1 and the glycosyl oxygen.
The products of the hydrolysis of sucrose and palatinose by the sucrase-isomaltase complex from rabbit small intestine were investigated by persilylation followed by gas-liquid chromatography and mass spectrometry. If the hydrolysis is carried out in H218O, the heavy oxygen is found exclusively at the Ci of the alpha-glucopyranose formed. The 18O enrichment equals that of the incubation medium....
متن کاملLocalization 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, ...
متن کاملAction of intestinal sucrase-isomaltase and its free monomers on an alpha-limit dextrin.
The concurrent action of the sucrase and isomaltase active sites of the hybrid sucrase-isomaltase from rat intestine on an a-limit dextrin was studied by use of 63 maltotriosylmaltotriose isolated from controlled action of pullulanase on pullulan. Hydrolysis of the a-dextrin hexasaccharide occurred by sequential removal of a glucose residue from its nonreducing end. The initial pentasaccharide ...
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ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1960
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.14-0072