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Extensive Disulfide Bonding at the Mammalian Cell Surface

Richard O. Hynes and Antonia Destree
Proceedings of the National Academy of Sciences of the United States of America
Vol. 74, No. 7 (Jul., 1977), pp. 2855-2859
Stable URL: http://www.jstor.org/stable/67260
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Extensive Disulfide Bonding at the Mammalian Cell Surface
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Abstract

Cell surface proteins of cultured cells are disulfide bonded to a greater degree than are total cellular proteins. In particular, the ``large external transformation-sensitive'' (LETS) protein, a major surface protein, is present almost exclusively in disulfide-bonded complexes including homodimers and also higher aggregates held together by disulfide bonds or noncovalent interactions. Other cell surface proteins also appear to be involved in disulfide bonding, both intramolecular and intermolecular. In virally transformed cells, LETS protein and its disulfide complexes are absent and certain other disulfidebonded proteins are also not observed.

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