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• W1516754372 startingPage "92" @default.
• W1516754372 abstract "The sucrase-isomaltase complex (SI) of the small intestinal brush border membrane accounts for approximately 9-10% of the intrinsic protein. The isomaltase subunit alone interacts with the membrane directly, via a highly hydrophobic segment at its N-terminal region. This segment has a helical conformation for more than 85% and crosses the membrane twice, the N-terminus being located at the outer, luminal side of the membrane. The sucrase subunit is attached to the membrane solely via its interactions with the isomaltase subunit. The sucrase-isomaltase complex is synthesized as a single, very long (Mr approximately 260 000) polypeptide chain (pro-SI, carrying the two sites of sucrase and isomaltase in an already enzymically active form), with the isomaltase portion corresponding to the N-terminal part of pro-SI. Pro-SI is processed into 'final' SI by pancreatic proteases. Recently the cell-free translation of pro-SI has been achieved in vitro. From a detailed knowledge of the anchoring of SI (and pro-SI) in the membrane it has been possible to suggest one particular mechanism as the most likely for the synthesis, insertion and assembly of pro-SI." @default.
• W1516754372 created "2016-06-24" @default.
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• W1516754372 creator A5091724579 @default.
• W1516754372 date "1983-01-01" @default.
• W1516754372 modified "2023-09-23" @default.
• W1516754372 title "Biosynthesis and Assembly of the Largest and Major Intrinsic Polypeptide of the Small Intestinal Brush Borders" @default.
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• W1516754372 doi "https://doi.org/10.1002/9780470720769.ch7" @default.
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• W1516754372 hasPublicationYear "1983" @default.
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