Biosynthesis of sucrase-isomaltase. Purification and NH2-terminal amino acid sequence of the rat sucrase-isomaltase precursor (pro-sucrase-isomaltase) from fetal intestinal transplants.

作者: H P Hauri , H Wacker , E E Rickli , B Bigler-Meier , A Quaroni

DOI: 10.1016/S0021-9258(18)34754-9

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摘要: The dimeric enzyme sucrase-isomaltase (a complex of sucrose alpha-glucohydrolase, EC 3.2.1.48 and oligo-1,6-glucosidase (dextrin 6 alpha-D-glucanohydrolase), 3.2.1.10) the rat small intestinal microvillus membrane is synthesized as a single chain enzymatically active precursor protein. This (called pro-sucrase-isomaltase) was purified from fetal transplants in which found almost exclusively uncleaved form. A two-step procedure developed using monoclonal antibody affinity chromatography on protein Sepharose CL-4B followed by preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. NH2-terminal sequence pro-sucrase-isomaltase identical with that isolated isomaltase subunit possesses anchor for mature but differed sucrase subunit. identity shows domain comprising prior to bulk destined be localized luminal side membrane. model proposed mode assembly subsequent cleavage into its subunits.

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