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• W1506131844 endingPage "5160" @default.
• W1506131844 startingPage "5154" @default.
• W1506131844 abstract "Insertion of the alpha- and beta-subunits of amphibian epithelial Na+,K+-ATPase into pancreatic microsomes in cell-free systems was shown to be the same as into membranes of intact cells. The glycoproteic beta-subunit was observed to be cotranslationally inserted into endoplasmic reticulum membranes and to adopt a different pattern of N-linked core and terminal sugars in two different amphibian species. The beta-subunit lacks a cleavable signal sequence but quantitative membrane integration required membrane addition at the start of synthesis. Proteolysis of beta-subunit assembled in vitro indicated a cleavable cytoplasmic domain of about 2000 daltons. The catalytic 98-kilodalton alpha-subunit was also membrane-associated during its synthesis in an alkali-resistant fashion and independent of newly synthesized beta-subunit. In contrast to the beta-subunit, membrane integration of the alpha-subunit was possible as late as a time point in its synthesis which corresponded to about 1/3-1/2 of completion of the nascent chain. A small 34 kDa trypsin-resistant fragment of the alpha-subunit was produced at an early stage of synthesis both in the intact cell and in the cell-free system. These results suggest that membrane insertion of both alpha- and beta-subunit occurs during their synthesis but with a different time course." @default.
• W1506131844 created "2016-06-24" @default.
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• W1506131844 date "1985-04-01" @default.
• W1506131844 modified "2023-10-18" @default.
• W1506131844 title "Membrane insertion of alpha- and beta-subunits of Na+,K+-ATPase." @default.
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• W1506131844 doi "https://doi.org/10.1016/s0021-9258(18)89192-x" @default.
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